Functional Organization of Sequence Motifs in Diverse Transit Peptides of Chloroplast Proteins

Although the chloroplasts in plants are characterized by an inherent genome, the chloroplast proteome is composed of proteins encoded by not only the chloroplast genome but also the nuclear genome. Nuclear-encoded chloroplast proteins are synthesized on cytosolic ribosomes and post-translationally t...

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Autores principales:	Jinseung Jeong, Inhwan Hwang, Dong Wook Lee
Formato:	article
Lenguaje:	EN
Publicado:	Frontiers Media S.A. 2021
Materias:	chloroplast transit peptide sequence motif protein targeting protein translocation Physiology QP1-981
Acceso en línea:	https://doaj.org/article/57c9a6fc93a845f1a479d4d14a593e3c
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spelling	oai:doaj.org-article:57c9a6fc93a845f1a479d4d14a593e3c2021-11-22T06:39:12ZFunctional Organization of Sequence Motifs in Diverse Transit Peptides of Chloroplast Proteins1664-042X10.3389/fphys.2021.795156https://doaj.org/article/57c9a6fc93a845f1a479d4d14a593e3c2021-11-01T00:00:00Zhttps://www.frontiersin.org/articles/10.3389/fphys.2021.795156/fullhttps://doaj.org/toc/1664-042XAlthough the chloroplasts in plants are characterized by an inherent genome, the chloroplast proteome is composed of proteins encoded by not only the chloroplast genome but also the nuclear genome. Nuclear-encoded chloroplast proteins are synthesized on cytosolic ribosomes and post-translationally targeted to the chloroplasts. In the latter process, an N-terminal cleavable transit peptide serves as a targeting signal required for the import of nuclear-encoded chloroplast interior proteins. This import process is mediated via an interaction between the sequence motifs in transit peptides and the components of the TOC/TIC (translocon at the outer/inner envelope of chloroplasts) translocons. Despite a considerable diversity in primary structures, several common features have been identified among transit peptides, including N-terminal moderate hydrophobicity, multiple proline residues dispersed throughout the transit peptide, preferential usage of basic residues over acidic residues, and an absence of N-terminal arginine residues. In this review, we will recapitulate and discuss recent progress in our current understanding of the functional organization of sequence elements commonly present in diverse transit peptides, which are essential for the multi-step import of chloroplast proteins.Jinseung JeongInhwan HwangDong Wook LeeDong Wook LeeFrontiers Media S.A.articlechloroplasttransit peptidesequence motifprotein targetingprotein translocationPhysiologyQP1-981ENFrontiers in Physiology, Vol 12 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	chloroplast transit peptide sequence motif protein targeting protein translocation Physiology QP1-981
spellingShingle	chloroplast transit peptide sequence motif protein targeting protein translocation Physiology QP1-981 Jinseung Jeong Inhwan Hwang Dong Wook Lee Dong Wook Lee Functional Organization of Sequence Motifs in Diverse Transit Peptides of Chloroplast Proteins
description	Although the chloroplasts in plants are characterized by an inherent genome, the chloroplast proteome is composed of proteins encoded by not only the chloroplast genome but also the nuclear genome. Nuclear-encoded chloroplast proteins are synthesized on cytosolic ribosomes and post-translationally targeted to the chloroplasts. In the latter process, an N-terminal cleavable transit peptide serves as a targeting signal required for the import of nuclear-encoded chloroplast interior proteins. This import process is mediated via an interaction between the sequence motifs in transit peptides and the components of the TOC/TIC (translocon at the outer/inner envelope of chloroplasts) translocons. Despite a considerable diversity in primary structures, several common features have been identified among transit peptides, including N-terminal moderate hydrophobicity, multiple proline residues dispersed throughout the transit peptide, preferential usage of basic residues over acidic residues, and an absence of N-terminal arginine residues. In this review, we will recapitulate and discuss recent progress in our current understanding of the functional organization of sequence elements commonly present in diverse transit peptides, which are essential for the multi-step import of chloroplast proteins.
format	article
author	Jinseung Jeong Inhwan Hwang Dong Wook Lee Dong Wook Lee
author_facet	Jinseung Jeong Inhwan Hwang Dong Wook Lee Dong Wook Lee
author_sort	Jinseung Jeong
title	Functional Organization of Sequence Motifs in Diverse Transit Peptides of Chloroplast Proteins
title_short	Functional Organization of Sequence Motifs in Diverse Transit Peptides of Chloroplast Proteins
title_full	Functional Organization of Sequence Motifs in Diverse Transit Peptides of Chloroplast Proteins
title_fullStr	Functional Organization of Sequence Motifs in Diverse Transit Peptides of Chloroplast Proteins
title_full_unstemmed	Functional Organization of Sequence Motifs in Diverse Transit Peptides of Chloroplast Proteins
title_sort	functional organization of sequence motifs in diverse transit peptides of chloroplast proteins
publisher	Frontiers Media S.A.
publishDate	2021
url	https://doaj.org/article/57c9a6fc93a845f1a479d4d14a593e3c
work_keys_str_mv	AT jinseungjeong functionalorganizationofsequencemotifsindiversetransitpeptidesofchloroplastproteins AT inhwanhwang functionalorganizationofsequencemotifsindiversetransitpeptidesofchloroplastproteins AT dongwooklee functionalorganizationofsequencemotifsindiversetransitpeptidesofchloroplastproteins AT dongwooklee functionalorganizationofsequencemotifsindiversetransitpeptidesofchloroplastproteins
_version_	1718418103060135936

Functional Organization of Sequence Motifs in Diverse Transit Peptides of Chloroplast Proteins

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