Auxiliary functions in photosynthesis: the role of the FtsH protease

被引:13
作者
Bailey, S [1 ]
Silva, P
Nixon, P
Mullineaux, C
Robinson, C
Mann, N
机构
[1] Univ Warwick, Dept Biol Sci, Coventry CV4 7AL, W Midlands, England
[2] Univ London Imperial Coll Sci Technol & Med, Dept Biochem, London SW7 2AY, England
[3] UCL, Dept Biol, London WC1E 6BT, England
关键词
FtsH; photoinhibition; photosynthesis; protease; reaction centre;
D O I
10.1042/BST0290455
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Oxygenic photosynthesis can be described effectively by using two long-standing models: the Z-scheme and the chemiosmotic hypothesis. However, these models do not reveal the dynamic nature of the thylakoid membrane and the four major complexes that it binds. The composition of the photosynthetic apparatus is continually changing in response to a range of environmental stimuli. In addition, many photosynthetic components have some of the highest turnover rates in Nature. Changes in composition and turnover of photosynthetic components require the degradation of existing and damaged polypeptides and the resynthesis and co-ordinated assembly of new polypeptides and their associated cofactors. This is achieved by several auxiliary functions, including proteolysis, protein targeting and the action of molecular chaperones. Some of the components involved in these functions, such as translocons, chaperones and proteases, have been identified but many of the auxiliary functions of photosynthesis remain uncharacterized. Among the proteases known to be associated with the thylakoids is the zinc metalloprotease FtsH, which might also act as a chaperone. Here we provide an overview of the thylakoid FtsH protease and discuss its role in the maintenance and assembly of the photosynthetic apparatus.
引用
收藏
页码:455 / 459
页数:5
相关论文
共 28 条
[1]   INVITRO STUDIES ON LIGHT-INDUCED INHIBITION OF PHOTOSYSTEM-II AND D1-PROTEIN DEGRADATION AT LOW-TEMPERATURES [J].
ARO, EM ;
HUNDAL, T ;
CARLBERG, I ;
ANDERSSON, B .
BIOCHIMICA ET BIOPHYSICA ACTA, 1990, 1019 (03) :269-275
[2]   DETECTION OF A 10 KDA BREAKDOWN PRODUCT CONTAINING THE C-TERMINUS OF THE D1-PROTEIN IN PHOTOINHIBITED WHEAT LEAVES SUGGESTS AN ACCEPTOR SIDE MECHANISM [J].
CANOVAS, PM ;
BARBER, J .
FEBS LETTERS, 1993, 324 (03) :341-344
[3]   Mutations in the Arabidopsis VAR2 locus cause leaf variegation due to the loss of a chloroplast FtsH protease [J].
Chen, M ;
Choi, YD ;
Voytas, DF ;
Rodermel, S .
PLANT JOURNAL, 2000, 22 (04) :303-313
[4]  
DUERLING E, 1997, J BACTERIOL, V177, P4105
[5]   PAS1, A YEAST GENE REQUIRED FOR PEROXISOME BIOGENESIS, ENCODES A MEMBER OF A NOVEL FAMILY OF PUTATIVE ATPASES [J].
ERDMANN, R ;
WIEBEL, FF ;
FLESSAU, A ;
RYTKA, J ;
BEYER, A ;
FROHLICH, KU ;
KUNAU, WH .
CELL, 1991, 64 (03) :499-510
[6]   Characterization of the stromal protease(s) degrading the cross-linked products of the D1 protein generated by photoinhibition of photosystem II [J].
Ferjani, A ;
Abe, S ;
Ishikawa, Y ;
Henmi, T ;
Tomokawa, Y ;
Nishi, Y ;
Tamura, N ;
Yamamoto, Y .
BIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS, 2001, 1503 (03) :385-395
[7]   IDENTIFICATION OF A PRIMARY INVIVO DEGRADATION PRODUCT OF THE RAPIDLY-TURNING-OVER 32-KD PROTEIN OF PHOTOSYSTEM-II [J].
GREENBERG, BM ;
GABA, V ;
MATTOO, AK ;
EDELMAN, M .
EMBO JOURNAL, 1987, 6 (10) :2865-2869
[8]   A chloroplast DegP2 protease performs the primary cleavage of the photodamaged D1 protein in plant photosystem II [J].
Kirsten Haußühl ;
Bertil Andersson ;
Iwona Adamska .
The EMBO Journal, 2001, 20 (4) :713-722
[9]   CELL-GROWTH AND LAMBDA-PHAGE DEVELOPMENT CONTROLLED BY THE SAME ESSENTIAL ESCHERICHIA-COLI GENE, FTSH HFLB [J].
HERMAN, C ;
OGURA, T ;
TOMOYASU, T ;
HIRAGA, S ;
AKIYAMA, Y ;
ITO, K ;
THOMAS, R ;
DARI, R ;
BOULOC, P .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1993, 90 (22) :10861-10865
[10]   Two ftsH-family genes encoded in the nuclear and chloroplast genomes of the primitive red alga Cyanidioschyzon merolae [J].
Itoh, R ;
Takano, H ;
Ohta, N ;
Miyagishima, S ;
Kuroiwa, H ;
Kuroiwa, T .
PLANT MOLECULAR BIOLOGY, 1999, 41 (03) :321-337