{"title":"叶绿体内蛋白酶:叶绿体蛋白水解的整体网络观点。","authors":"Klaas J van Wijk","doi":"10.1093/plcell/koae178","DOIUrl":null,"url":null,"abstract":"<p><p>Different proteases and peptidases are present within chloroplasts and nonphotosynthetic plastids to process precursor proteins and to degrade cleaved chloroplast transit peptides and damaged, misfolded, or otherwise unwanted proteins. Collectively, these proteases and peptidases form a proteolysis network, with complementary activities and hierarchies, and build-in redundancies. Furthermore, this network is distributed across the different intra-chloroplast compartments (lumen, thylakoid, stroma, envelope). The challenge is to determine the contributions of each peptidase (system) to this network in chloroplasts and nonphotosynthetic plastids. This will require an understanding of substrate recognition mechanisms, degrons, substrate, and product size limitations, as well as the capacity and degradation kinetics of each protease. Multiple extra-plastidial degradation pathways complement these intra-chloroplast proteases. This review summarizes our current understanding of these intra-chloroplast proteases in Arabidopsis and crop plants with an emphasis on considerations for building a qualitative and quantitative network view.</p>","PeriodicalId":20186,"journal":{"name":"Plant Cell","volume":" ","pages":"3116-3130"},"PeriodicalIF":10.0000,"publicationDate":"2024-09-03","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11371162/pdf/","citationCount":"0","resultStr":"{\"title\":\"Intra-chloroplast proteases: A holistic network view of chloroplast proteolysis.\",\"authors\":\"Klaas J van Wijk\",\"doi\":\"10.1093/plcell/koae178\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><p>Different proteases and peptidases are present within chloroplasts and nonphotosynthetic plastids to process precursor proteins and to degrade cleaved chloroplast transit peptides and damaged, misfolded, or otherwise unwanted proteins. Collectively, these proteases and peptidases form a proteolysis network, with complementary activities and hierarchies, and build-in redundancies. Furthermore, this network is distributed across the different intra-chloroplast compartments (lumen, thylakoid, stroma, envelope). The challenge is to determine the contributions of each peptidase (system) to this network in chloroplasts and nonphotosynthetic plastids. This will require an understanding of substrate recognition mechanisms, degrons, substrate, and product size limitations, as well as the capacity and degradation kinetics of each protease. Multiple extra-plastidial degradation pathways complement these intra-chloroplast proteases. This review summarizes our current understanding of these intra-chloroplast proteases in Arabidopsis and crop plants with an emphasis on considerations for building a qualitative and quantitative network view.</p>\",\"PeriodicalId\":20186,\"journal\":{\"name\":\"Plant Cell\",\"volume\":\" \",\"pages\":\"3116-3130\"},\"PeriodicalIF\":10.0000,\"publicationDate\":\"2024-09-03\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11371162/pdf/\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Plant Cell\",\"FirstCategoryId\":\"99\",\"ListUrlMain\":\"https://doi.org/10.1093/plcell/koae178\",\"RegionNum\":1,\"RegionCategory\":\"生物学\",\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"Q1\",\"JCRName\":\"BIOCHEMISTRY & MOLECULAR BIOLOGY\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Plant Cell","FirstCategoryId":"99","ListUrlMain":"https://doi.org/10.1093/plcell/koae178","RegionNum":1,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q1","JCRName":"BIOCHEMISTRY & MOLECULAR BIOLOGY","Score":null,"Total":0}
Intra-chloroplast proteases: A holistic network view of chloroplast proteolysis.
Different proteases and peptidases are present within chloroplasts and nonphotosynthetic plastids to process precursor proteins and to degrade cleaved chloroplast transit peptides and damaged, misfolded, or otherwise unwanted proteins. Collectively, these proteases and peptidases form a proteolysis network, with complementary activities and hierarchies, and build-in redundancies. Furthermore, this network is distributed across the different intra-chloroplast compartments (lumen, thylakoid, stroma, envelope). The challenge is to determine the contributions of each peptidase (system) to this network in chloroplasts and nonphotosynthetic plastids. This will require an understanding of substrate recognition mechanisms, degrons, substrate, and product size limitations, as well as the capacity and degradation kinetics of each protease. Multiple extra-plastidial degradation pathways complement these intra-chloroplast proteases. This review summarizes our current understanding of these intra-chloroplast proteases in Arabidopsis and crop plants with an emphasis on considerations for building a qualitative and quantitative network view.
期刊介绍:
Title: Plant Cell
Publisher:
Published monthly by the American Society of Plant Biologists (ASPB)
Produced by Sheridan Journal Services, Waterbury, VT
History and Impact:
Established in 1989
Within three years of publication, ranked first in impact among journals in plant sciences
Maintains high standard of excellence
Scope:
Publishes novel research of special significance in plant biology
Focus areas include cellular biology, molecular biology, biochemistry, genetics, development, and evolution
Primary criteria: articles provide new insight of broad interest to plant biologists and are suitable for a wide audience
Tenets:
Publish the most exciting, cutting-edge research in plant cellular and molecular biology
Provide rapid turnaround time for reviewing and publishing research papers
Ensure highest quality reproduction of data
Feature interactive format for commentaries, opinion pieces, and exchange of information in review articles, meeting reports, and insightful overviews.