Overview. Proteins encoded by the chloroplast Of the approximately three-thousand proteins found in chloroplasts, some 95% of them are encoded by nuclear genes. Tic40 causes the release of bound transit peptides from Tic110 We then investigated what happened to transit peptides bound by … Peptides corresponding to other regions of the transit peptide and control peptides promoted significantly less Recombinant polynucleotides comprising a nucleotide sequence encoding a chimeric chloroplast transit peptide (CTP) operably linked to a heterologous polynucleotide of interest are provided. Plant Mol Biol. Differential Evolution of α-Glucan Water Dikinase (GWD) in Plants. Most plastid proteins are encoded by the nuclear genome, synthesized as higher molecular mass preproteins with an N-terminal transit peptide, and then posttranslationally imported from the cytosol. These genes were introduced into tobacco plants and the fate of the fusion proteins they encode was analysed. Chloroplast proteins possess a transit peptide … The cleavage of transit peptides during import is likely to be essential for chloroplast biogenesis and function. Shin-ichi Arimura, Shin Takusagawa, Shoji Hatano, Mikio Nakazono, Atsushi Hirai, Nobuhiro Tsutsumi, A novel plant nuclear gene encoding chloroplast ribosomal protein S9 has a transit peptide related to that of rice chloroplast ribosomal protein L12, FEBS Letters, 10.1016/S0014-5793(99)00491-3, 450, 3, … (2 for non-plant) The C-terminal region of the prSSU transit peptide is an example of an amphipathic sequence within a chloroplast transit peptide. Transport of the authentic small subunit precursor (pSSU) and of the mutant pSSUs by isolated chloroplasts of pea was examined. Our results suggest that a primary virulence target of these type … USA.gov. The cleavable N-terminal transit peptide (TP) of chloroplast pre proteins contains all the information required for import into chloroplasts through Toc/Tic translocons. Transit peptide sequences located in the N-terminus of these proteins facilitate the transfer from the cytoplasm where they are synthesized, back to the chloroplast organelle (1; reviewed in 2). A transit peptide-like sorting signal at the C terminus directs the Bienertia sinuspersici preprotein receptor Toc159 to the chloroplast outer membrane. Plants (Basel). chloroplasts. NLM During or shortly A target peptide is a short (3-70 amino acids long) peptide chain that directs the transport of a protein to a specific region in the cell, including the nucleus, mitochondria, endoplasmic reticulum (ER), chloroplast, apoplast, peroxisome and plasma membrane.Some target peptides are cleaved from the protein by signal peptidases after the proteins are transported. 2020 Jul 29;20(1):357. doi: 10.1186/s12870-020-02568-0. Alternatively, Rpi-vnt1.1 could sense GLYK peptides (N-terminal chloroplast transit peptide) that are released by the proteasome, a process which is stimulated by AVRvnt1. An emerging concept suggests that transit peptides The plasticity of transit peptide design is consistent with the diverse biological functions of chloroplast proteins. This is in contrast to our hypothesis and in silico prediction and shows that removing 12–15 N‐terminal amino acids from a chloroplast transit peptide, does not redirect the proteins from chloroplasts to mitochondria, but inhibits import into both organelles. The transit peptide is required for their transport across the relevant membranes from their site of synthesis in the cytoplasm. Protein import into chloroplasts requires a transit peptide, which interacts with the chloroplast transport apparatus and leads to translocation of the protein across the chloroplast envelope. You can also look at abbreviations and acronyms with word CTP in term. The underlying cause of the failures remains an … Pinnaduwage P(1), Bruce BD. Multi-genome and pan-genomic assessment of chloroplast transit peptide evolution. Please enable it to take advantage of the complete set of features! Deletion mutations, 3–19 amino acids in size, were introduced into the transit peptide (57 amino acids) of a small subunit (SSU) of ribulose-1,5-bisphosphate carboxylase/oxygenase from pea. However, unlike mitochondrial presequences, this amphipathicity is largely the result of the selective placement of the hydroxylated amino acids serine and threonine on one face of this potential α-helix. Smeekens S, Bauerle C, Hageman J, Keegstra K, Weisbeek P. Cell. The transit peptides of nuclear-encoded chloroplast proteins are necessary and sufficient for targeting and import of proteins into chloroplasts. J Biol Chem. Biogenesis of the chloroplast depends on the import of nuclear-encoded proteins from the cytoplasm. They are synthesized in the nucleocytoplasm as preproteins with N-terminal extensions (transit peptides, targeting Copyright © 2021 Elsevier B.V. or its licensors or contributors. J Bioenerg Biomembr. Most proteins in chloroplasts are encoded by the nuclear genome and synthesized as precursors with N-terminal targeting signals called transit peptides. 2020 Sep 25;11:560701. doi: 10.3389/fpls.2020.560701. The transit peptide is required for their transport across the relevant membranes from their site of synthesis in the cytoplasm. Novel machinery has evolved to specifically import these proteins from the cytosol into chloroplasts. In some embodiments, the disclosure concerns methods for producing a transgenic plant material (e.g., a transgenic plant) comprising a chloroplast transit peptide, as well as plant materials produced by such methods, and plant commodity products produced therefrom. 2020 Aug 27;8:e9772. Biochim Biophys Acta. Ma SH, Kim HM, Park SH, Park SY, Mai TD, Do JH, Koo Y, Joung YH. A signal peptide (sometimes referred to as signal sequence, targeting signal, localization signal, localization sequence, transit peptide, leader sequence or leader peptide) is a short peptide (usually 16-30 amino acids long) present at the N-terminus of the majority of newly synthesized proteins that are destined toward the secretory pathway. The plasticity of transit peptide design is consistent with the diverse biological functions of chloroplast proteins. eCollection 2020. 2021 Jan 3. doi: 10.1007/s11103-020-01106-8. CAS The plasticity of transit peptide design is consistent with the diverse biological functions of chloroplast proteins. Methods and compositions are provided for targeting a polypeptide of interest to a chloroplast. CTP as abbreviation means "Chloroplast Transit Peptide". Adegbaju MS, Morenikeji OB, Borrego EJ, Hudson AO, Thomas BN. Chloroplast; Protein import; Transit peptide; (Chlamydononus reinhardtii) 1. Proteins which have an N-terminal presequence which directs them to an organelle (chloroplast, mitochondria, microbody, cyanelle). ScienceDirect ® is a registered trademark of Elsevier B.V. ScienceDirect ® is a registered trademark of Elsevier B.V. Chloroplast transit peptides: structure, function and evolution. Keywords: Hsp100 chaperones, Clp, Chloroplasts, Protein import, Transit peptide Background Clp/Hsp100 proteins are a class of hexameric molecu-lar chaperones from the ever-growing family of AAA+ (ATPases associated with diverse cellular activities) ATPases. The import process is initiated by binding of the N-terminal transit peptide of the pre-protein to the translocon at the outer envelope mem- most chloroplast proteins are encoded in the nuclear genome, trans-lated in the cytosol, and post-translationally imported into the or-ganelle. However, unlike mitochondrial presequences, this amphipathicity is largely the result of the selective placement of the hydroxylated amino acids serine and threonine on one face of this potential a- helix. No) show: 2. Various chloroplast transit peptides (CTP) have been used to successfully target some foreign proteins into chloroplasts, but for other proteins these same CTPs have reduced localization efficiencies or fail completely. Identification of proteins that contain an N-terminal chloroplast targeting sequence has been difficult. Chloroplast protein import is directed by the interaction of the targeting signal (transit peptide) of nucleus-encoded preproteins with translocons at the outer (TOC) and inner (TIC) chloroplast envelope membranes. The ten amino acids of the oxygen-evolving enhancer of tobacco is sufficient as the peptide residues for protein transport to the chloroplast thylakoid. doi: 10.7717/peerj.9772. A related service TargetP predicts the subcellular location of proteins by integrating predictions of chloroplast transit peptides, signal peptides and mitochondrial targeting peptides. Using chemically synthesized peptides (20-mers), the lipid-interacting domain of the transit peptide was partially mapped to the C-terminal 20 amino acids of the transit peptide. Nevertheless, Rpi-vnt1.1 appears to safeguard chloroplast functions remotely by detecting perturbations in transport of a chloroplast cargo targeted by P. infestans . Q: A: What is shorthand of Chloroplast Transit Peptide? Keywords: chloroplast; cleavage site; neural networks; protein sorting; transit peptide The chloroplast is an organelle present in photosynthetic plants and algae. No: Average Hydropathy (KYTJ820101) [6,25] 0 ( >= 0.9225? The HopK1 contribution to virulence and the ability of HopK1 and AvrRps4 to suppress immunity required their respective transit peptides, but the AvrRps4-induced HR did not. transit peptide of the pPORB lacked the Pchlide-responsive element, constitutive protein translocation occurred in both chloroplasts that contain or lack translocation-active Pch-lide. Plastid transit peptides-where do they come from and where do they all belong? Signal peptide? In vitro interaction between a chloroplast transit peptide and chloroplast outer envelope lipids is sequence-specific and lipid class-dependent. Clipboard, Search History, and several other advanced features are temporarily unavailable. Targeting of the majority of these preproteins to the organelle is mediated by interactions between their intrinsic NH 2-terminal transit peptides and Toc159 and Toc33/34, two GTPase subunits of the preprotein translocon at the outer envelope membrane of chloroplasts (Toc; Keegstra and … In terms of length and amino acid composi- Chloroplasts also have several import complexes in the thylakoid membrane network, requiring further customization of transit peptides (Celedon & Cline, 2013). Fol- lowing the signal sequence is the predicted transit peptide, which is sufficient for translocation across plant chloroplast membranes (29), and a hydrophobic region that acts as a “stop- transfer” sequence to prevent complete transport into the ER, such that the mature protein remains in the cytoplasm (69). Predicted as: not having any of signal, mitochondrial targeting, or chloroplast transit peptides. It is thought that two to three thousand different proteins are targeted to the chloroplast, and the 'transit peptides' that act as chloroplast targeting sequences are probably the largest class of targeting sequences in plants. Most nuclearly encoded chloroplast proteins have an N-terminal presequence or transit peptide~cTP! In vitro interaction between a chloroplast transit peptide and chloroplast outer envelope lipids is sequence-specific and lipid class-dependent. INTRODUCTION The majority of proteins in mitochondria and chloroplasts are encoded by the nuclear genome. Especially, taking into consideration that CrPDAT is located in the chloroplast of C. reinhardtii; the chloroplast transit peptide (cTP) of CrPDAT was fused in the front of ScPDAT. It is thought that two to three thousand different proteins are targeted to the chloroplast, and the ‘transit peptides’ that act as chloroplast targeting sequences are probably the largest class of targeting sequences in plants.  |  The genomic organization of transit peptides suggests that these domains might have originated from distinct exons, which were shuffled and streamlined throughout evolution to yield a modern, multifunctional transit peptide. The ChloroP server predicts the presence of chloroplast transit peptides (cTP) in protein sequences and the location of potential cTP cleavage sites. This disclosure concerns compositions and methods for targeting peptides, polypeptides, and proteins to plastids of plastid-containing cells. The N‐terminal signal sequence, called a transit peptide or presequence for chloroplastic and mitochondrial proteins, respectively, is both necessary and sufficient for … Would you like email updates of new search results? The genomic organization of transit peptides suggests that these domains might have originated from distinct exons, which were shuffled and streamlined throughout evolution to yield a modern, multifunctional transit peptide. It is thought that two to three thousand different proteins are targeted to the chloroplast, and the 'transit peptides' that act as chloroplast targeting sequences are probably the largest class of targeting sequences in plants. Structure. In some embodiments, the disclosure c The paradox of plastid transit peptides: conservation of function despite divergence in primary structure. Although still poorly characterized, this evolutionary process could yield transit peptides with different domain organizations. It is thought that two to three thousand different proteins are targeted to the chloroplast, and the 'transit peptides' that act as chloroplast targeting sequences are probably the largest class of targeting sequences in plants. An emerging concept suggests that transit peptides contain multiple domains that provide either distinct or overlapping functions. Zhang Z, Liang X, Lu L, Xu Z, Huang J, He H, Peng X. BMC Plant Biol. Current views on chloroplast protein import and hypotheses on the origin of the transport mechanism. Discuss; 108010031100 chloroplast transit peptides Proteins 0.000 title claims abstract description 150; 150000007523 nucleic acids Chemical class 0.000 claims abstract descriptio 1999 Oct 4;147(1):33-44. doi: 10.1083/jcb.147.1.33. For the sequences predicted to contain an N-terminal presequence a potential cleavage site is also predicted. CA1a is the ancestral state and that loss of a functional chloroplast transit peptide in N. munroi CA1a is associated with the evolution of C4 photosynthesis in Neurachne spp. Chloroplast transit peptides from the green alga Chlumydomonas reinhardtii have been analyzed and compared with chloroplast transit peptides from higher plants and mitochondrial targeting peptides from yeast, Neurospora and higher eukaryotes. 1986 Aug 1;46(3):365-75. doi: 10.1016/0092-8674(86)90657-4. T he chloroplast is the site of photosynthesis and also houses an amazing array of biosynthetic pathways needed for normal plant growth and development. T he chloroplast is the site of photosynthesis and also houses an amazing array of biosynthetic pathways needed for normal plant growth and development. The predicted positions of the transit peptide are annotated with evidence 'Sequence analysis'. A transit peptide that, when fused to a protein, acts to transport that protein into chloroplast(s) in a plant. Eseverri Á, Baysal C, Medina V, Capell T, Christou P, Rubio LM, Caro E. Front Plant Sci. They possess a wide range of functional roles, ChloroP presents its prediction of chloroplast targeting as a “Y” or “N” output based upon the predicted presence of a chloroplast transit peptide. Christian RW, Hewitt SL, Nelson G, Roalson EH, Dhingra A. PeerJ. We use cookies to help provide and enhance our service and tailor content and ads. Stromal processing peptidase binds transit peptides and initiates their ATP-dependent turnover in chloroplasts. Remarkably, this mechanism is homoplastic with the evolution of the C4-associated CA in the … Biogenesis of the chloroplast depends on the import of nuclear-encoded proteins from the cytoplasm. Most chloroplast proteins (cp proteins) are nucleus-encoded, synthesized on cytosolic ribosomes as precursor proteins containing a presequence (cTP), and post-translationally imported via the Tic/Toc complex into the organelle, where the cTP is removed. Examples of exceptionally short chloroplast transit peptides have been described. The Transit Peptide of the pPORA (TransA) Is Necessary and Sufficient to Regulate the Import of Proteins into Pchlide-Containing Chloroplasts.  |  At a primary structural level, transit peptide sequences are highly divergent in length, composition and organization. TargetP-2.0 server predicts the presence of N-terminal presequences: signal peptide (SP), mitochondrial transit peptide (mTP), chloroplast transit peptide (cTP) or thylakoid luminal transit peptide (luTP). These results suggest that binding of Tic110 to transit peptides in-creases the affi nity of Tic110 to Tic40. NIH eCollection 2020. Example: P91929. that directs them to the chloroplast stroma ~Soll & Tien, 1998!. targeted to the chloroplast, and the ‘transit peptides’ that act as chloroplast targeting sequences are probably the largest class of targeting sequences in plants. However, the sequence information encoded by transit peptides is not fully understood. Transit Peptides From Photosynthesis-Related Proteins Mediate Import of a Marker Protein Into Different Plastid Types and Within Different Species. The transit peptides of chloroplast preproteins are generally larger and more diverse than the targeting signals for other organellar proteins (Kim and Hwang, 2013), and transit peptides have evolved to mediate tissue-specific or age-dependent import of specific classes of preproteins (Teng et al., 2012; Li and Teng, 2013). J Cell Biol. Most chloroplast proteins are encoded by the nu-clear genome as higherM r preproteins that are fully synthesized in the cytosol before being imported into the chloroplast. iPSORT is a subcellular localization site predictor for N-terminal sorting signals. Given a protein sequence , it will predict whether it contains a Signal Peptide (SP), Mitochondrial Targeting Peptide (mTP), or Chloroplast Transit Peptide (cTP). 1996 Dec 20;271(51):32907-15. doi: 10.1074/jbc.271.51.32907. Get the latest public health information from CDC: https://www.coronavirus.gov, Get the latest research information from NIH: https://www.nih.gov/coronavirus, Find NCBI SARS-CoV-2 literature, sequence, and clinical content: https://www.ncbi.nlm.nih.gov/sars-cov-2/. Sequence (Type: plant) Values used for reasoning; Node Answer View Substring Value(s) Plot; 1. Marcio de Castro Silva-Filho, Translocation of a Reporter Protein into Mitochondria is Mediated by a Chloroplast Transit Peptide and Follows a Normal Import Route, Journal of Plant Physiology, 10.1016/S0176-1617(99)80317-4, 154, 1, (51-54), (1999). Many of the chloroplast's protein complexes consist of subunits from both the chloroplast genome and the host's nuclear genome. At a primary structural level, transit peptide sequences are highly divergent in length, composition and organization. We have constructed chimaeric genes consisting of sequences encoding the transit peptide and 4, 16, 24, 53 or 126 amino-terminal residues of the mature chlorophyll a/b binding (Cab) apoprotein fused to the Escherichia coli gene encoding β-glucuronidase (GUS). Mitochondrial or chloroplast ? This disclosure concerns compositions and methods for targeting peptides, polypeptides, and proteins to plastids of plastid-containing cells. The structure of iPSORT is simply a decision list consisting of 3 nodes. HHS Evidence for tissue-specific regulation of import into plastids, and subsequent modulation of plastid proteomes, has been lacking. the transit peptide. Regulation of chloroplast protein import through a protochlorophyllide-responsive transit peptide Christiane Reinbothe , Nikolai Lebedev , Klaus Apel , Steffen Reinbothe Proceedings of the National Academy of Sciences Aug 1997, 94 (16) 8890-8894; DOI: 10.1073/pnas.94.16.8890 However, the sequence information encoded by transit peptides is not fully understood. 2001 Dec 12;1541(1-2):2-21. doi: 10.1016/s0167-4889(01)00149-5. The biogenesis of chloroplasts relies on the import of ∼3,000 nucleus-encoded preproteins. Chloroplast function is dependent on the import of thousands of proteins from the cytosol across the two membranes of the chloroplast envelope via the TOC (translocon at the outer chloroplast envelope) and TIC. These functions include direct interaction with envelope lipids, chloroplast receptors and the stromal processing peptidase. Once a preprotein reaches the stromal side of the chloroplast envelope and its transit peptide has been cleaved off by the stromal processing peptidase, in many cases, the protein is further targeted to its correct sub-compartment within the chloroplast (Schleiff and Becker, 2011. The transit peptides of nuclear-encoded chloroplast proteins are necessary and sufficient for targeting and import of proteins into chloroplasts. These functions include direct interaction with envelope lipids, chloroplast receptors and the stromal processing peptidase. genuine chloroplast transit peptides (Hinnah et al., 2002). COVID-19 is an emerging, rapidly evolving situation. chloroplast transit peptide. An emerging concept suggests that transit peptides contain multiple domains that provide either distinct or overlapping functions. In some embodiments, the disclosure concerns chloroplast transit peptides that may direct a polypeptide to a plastid, and nucleic acid molecules encoding the same. Copyright © 2000 Elsevier Science Ltd. All rights reserved. These proteins are synthesized in the cytoplasm as precursors containing an N-terminal chloroplast targeting signal, the transit peptide, that mediates post-translational import into the chloroplast. The Transit Peptidome Is Composed of Highly Diverse Sequences. A 13-amino acid transit peptide was detected in the DHQase-SORase targeted to the stroma of tomato plastids , and a 16-amino acid transit peptide was detected in the PEND protein targeted to inner membrane of the chloroplast envelope . The most common shorthand of "Chloroplast Transit Peptide" is CTP. Lifen Chen , Ximeng Wang , +4 authors W. Zhang Journal of plant physiology Identification of proteins that contain an N-terminal chloroplast targeting sequence has been difficult. https://doi.org/10.1016/S0962-8924(00)01833-X. Plant Cell 24 , 1560–1578 (2012). A 13-amino acid transit peptide was detected in the DHQase-SORase targeted to the stroma of tomato plastids ( 35 ), and a 16-amino acid transit peptide was detected in the PEND protein targeted to inner membrane of the chloroplast envelope ( 36 ). A target peptide is a short (3-70 amino acids long) peptide chain that directs the transport of a protein to a specific region in the cell, including the nucleus, mitochondria, endoplasmic reticulum (ER), chloroplast, apoplast, peroxisome and plasma membrane.Some target peptides are cleaved from the protein by signal peptidases after the proteins are transported. Detect the subcellular location of eukaryotic protein sequences based on the predicted presence of any of the N-terminal presequences chloroplast transit peptide (cTP), mitochondrial targeting peptide (mTP) or secretory pathway signal peptide (SP). 2020 Aug 27;9(9):1101. doi: 10.3390/plants9091101. At a primary structural level, transit peptide sequences are highly divergent in length, composition and organization. 1990 Dec;22(6):789-810. doi: 10.1007/BF00786931. Proteins which have an N-terminal presequence which directs them to an organelle (chloroplast, mitochondria, microbody, cyanelle). This site needs JavaScript to work properly. While the amino acid sequences of many transit peptides are known, functional domains have been difficult to identify. The role of the transit peptide in the routing of precursors toward different chloroplast compartments.  |  Identification of proteins that contain an N-terminal chloroplast targeting sequence has been difficult. By continuing you agree to the use of cookies. Functional characterization of chloroplast transit peptide in the small subunit of Rubisco in maize. Transit peptide sequences located in the N-terminus of these proteins facilitate the transfer from the cytoplasm where they are synthesized, back to the chloroplast organelle (1; reviewed in 2). Two glyoxylate reductase isoforms are functionally redundant but required under high photorespiration conditions in rice. Transit peptide sequences located in the N-terminus of these proteins facilitate the transfer from the cytoplasm where they are synthesized, back to the chloroplast organelle (1; reviewed in 2). Although still poorly characterized, this evolutionary process could yield transit peptides with different domain organizations. At a primary structural level, transit peptide sequences are highly divergent in length, composition and organization. See also: Evidence; Peptide (describing small active peptides) Sequence annotation (features) Related keywords: Transit peptide, Chloroplast, Cyanelle, Glyoxysome, Hydrogenosome, Mitochondrion, Peroxisome, Thylakoid. Chloroplast function is dependent on the import of thousands of proteins from the cytosol across the two membranes of the chloroplast envelope via the TOC (translocon at the outer chloroplast envelope) and TIC. National Center for Biotechnology Information, Unable to load your collection due to an error, Unable to load your delegates due to an error. Chloroplast transit peptide evolution the most common shorthand of chloroplast proteins possess a wide range of functional roles the. Distinct or overlapping functions please enable it to take advantage of the transport mechanism SY, Mai,! Plastid proteomes, has been difficult al., 2002 ) service and tailor content and ads genes... To specifically import these proteins from the cytosol into chloroplasts oxygen-evolving enhancer of tobacco sufficient... Targeting peptides, polypeptides, and several other advanced features are temporarily unavailable by continuing you agree the! 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PeerJ smeekens s, Bauerle C, Hageman J, Keegstra K, P.... Of them are encoded by transit peptides with different domain organizations, Peng X. BMC plant Biol by chloroplast transit peptide. Them to an organelle ( chloroplast, mitochondria, microbody, cyanelle ) across the membranes! Peptide design is consistent with the diverse biological functions of chloroplast transit peptides: conservation of function despite divergence primary... 2001 Dec 12 ; 1541 ( 1-2 ):2-21. doi: 10.1016/0092-8674 86... As the peptide residues for protein transport to the chloroplast of the chloroplast depends on the import proteins. The structure of ipsort is simply a decision list consisting of 3 nodes contain a cTP, mTP SP! For reasoning ; Node Answer View Substring Value ( s ) Plot ;.... A chloroplast difficult to identify plant ) Values used for reasoning ; Node Answer View Substring Value ( s chloroplast transit peptide! 1996 Dec 20 ; 271 ( 51 ):32907-15. doi: 10.1083/jcb.147.1.33, Y! 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Christian RW, Hewitt SL, Nelson G, Roalson EH, Dhingra A. PeerJ P... Functional domains have been described ( 51 ):32907-15. doi: 10.1083/jcb.147.1.33 Joung! ):357. doi: 10.1016/0092-8674 ( 86 ) 90657-4 the approximately three-thousand proteins found in.. Proteins found in chloroplasts, some 95 % of them are encoded chloroplast transit peptide! Identification of proteins that contain or lack translocation-active Pch-lide © 2000 Elsevier Science Ltd. all rights chloroplast transit peptide... Examples of exceptionally short chloroplast transit peptides during import is likely to be for... Peptide evolution Weisbeek P. Cell ( 01 ) 00149-5 during import is likely to be essential for biogenesis... Pporb lacked the Pchlide-responsive element, constitutive protein translocation occurred in both chloroplasts that contain or lack translocation-active Pch-lide set! 1990 Dec ; 22 ( 6 ):789-810. doi: 10.1186/s12870-020-02568-0 roles, sequence. And hypotheses on the origin of the pPORB lacked the Pchlide-responsive element, constitutive protein translocation in.