Chloroplast and Mitochondrial Proteases in Arabidopsis. A Proposed Nomenclature

Author:

Adam Zach1,Adamska Iwona2,Nakabayashi Kazumi3,Ostersetzer Oren1,Haussuhl Kirsten2,Manuell Andrea4,Zheng Bo5,Vallon Olivier6,Rodermel Steven R.4,Shinozaki Kazuo7,Clarke Adrian K.8

Affiliation:

1. Department of Agricultural Botany, The Hebrew University of Jerusalem, Rehovot 76100, Israel (Z.A., O.O.);

2. Department of Biochemistry, Arrhenius Laboratories for Natural Sciences, Stockholm University, S–10691 Stockholm, Sweden (I.A., K.H.);

3. Department of Biological Sciences, Graduate School of Science, University of Tokyo, Hongo, Bunkyo-ku, Tokyo, 113–0033 Japan (K.N.);

4. Department of Botany, Iowa State University, Ames, Iowa 50011 (A.M., S.R.R.);

5. Department of Plant Physiology, University of Umeå, S–901 87 Umeå, Sweden (B.Z.);

6. Institut de Biologie Physico-Chimique, Centre National de la Recherche Scientifique, Unité Propre de Recherche 1261, F–75005 Paris, France (O.V.);

7. Laboratory of Plant Molecular Biology, The Institute of Physical and Chemical Research, Koyadai, Tsukuba, Ibaraki, 305–0074 Japan (K.S.); and

8. Botanical Institute, Göteborg University, S–405 30 Göteborg, Sweden (A.K.C).

Abstract

Abstract The identity and scope of chloroplast and mitochondrial proteases in higher plants has only started to become apparent in recent years. Biochemical and molecular studies suggested the existence of Clp, FtsH, and DegP proteases in chloroplasts, and a Lon protease in mitochondria, although currently the full extent of their role in organellar biogenesis and function remains poorly understood. Rapidly accumulating DNA sequence data, especially from Arabidopsis, has revealed that these proteolytic enzymes are found in plant cells in multiple isomeric forms. As a consequence, a systematic approach was taken to catalog all these isomers, to predict their intracellular location and putative processing sites, and to propose a standard nomenclature to avoid confusion and facilitate scientific communication. For the Clp protease most of the ClpP isomers are found in chloroplasts, whereas one is mitochondrial. Of the ATPase subunits, the one ClpD and two ClpC isomers are located in chloroplasts, whereas both ClpX isomers are present in mitochondria. Isomers of the Lon protease are predicted in both compartments, as are the different forms of FtsH protease. DegP, the least characterized protease in plant cells, has the most number of isomers and they are predicted to localize in several cell compartments. These predictions, along with the proposed nomenclature, will serve as a framework for future studies of all four families of proteases and their individual isomers.

Publisher

Oxford University Press (OUP)

Subject

Plant Science,Genetics,Physiology

Reference37 articles.

1. Protein stability and degradation in chloroplasts.;Adam;Plant Mol Biol,1996

2. Chloroplast proteases and their role in photosynthesis regulation.;Adam,2000

3. Chloroplast proteases: possible regulators of gene expression?;Adam;Biochimie,2000

4. Gapped BLAST and PSI-BLAST: a new generation of protein database search programs.;Altschul;Nucleic Acids Res,1997

5. Proteolytic activities and proteases of plant chloroplasts.;Andersson;Physiol Plant,1997

同舟云学术

1.学者识别学者识别

2.学术分析学术分析

3.人才评估人才评估

"同舟云学术"是以全球学者为主线,采集、加工和组织学术论文而形成的新型学术文献查询和分析系统,可以对全球学者进行文献检索和人才价值评估。用户可以通过关注某些学科领域的顶尖人物而持续追踪该领域的学科进展和研究前沿。经过近期的数据扩容,当前同舟云学术共收录了国内外主流学术期刊6万余种,收集的期刊论文及会议论文总量共计约1.5亿篇,并以每天添加12000余篇中外论文的速度递增。我们也可以为用户提供个性化、定制化的学者数据。欢迎来电咨询!咨询电话:010-8811{复制后删除}0370

www.globalauthorid.com

TOP

Copyright © 2019-2024 北京同舟云网络信息技术有限公司
京公网安备11010802033243号  京ICP备18003416号-3