A novel protein for photosystem I biogenesis

被引:71
作者
Stöckel, J [1 ]
Oelmüller, R [1 ]
机构
[1] Univ Jena, Inst Allgemeine Bot & Pflanzenphysiol, D-07747 Jena, Germany
关键词
D O I
10.1074/jbc.M309246200
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
Hcf101-1 is a high-chlorophyll-fluorescence (hcf) Arabidopsis mutant that lacks photosystem I ( 1). Photosystem I subunits are synthesized in the mutant but do not assemble into a stable complex. hcf101 was isolated by map-based cloning and encodes an MRP-like protein with a nucleotide-binding domain. The protein is localized in the chloroplast stroma. In green tissue, the Hcf101 level is stimulated by light, and the protein is not detectable in roots. Two independent knock-out lines, hcf101-2 and hcf101-3, are also impaired in Hcf101 accumulation, although to different extents. Like hcf101-1, hcf101-2 and hcf01-3 are hcf mutants with impaired photosystem I. Our results indicate that Hcf101 is a novel component required for photosystem I biosynthesis.
引用
收藏
页码:10243 / 10251
页数:9
相关论文
共 74 条
[71]   MUTATIONAL ANALYSIS OF PHOTOSYSTEM-I POLYPEPTIDES IN THE CYANOBACTERIUM SYNECHOCYSTIS SP, PCC-6803 - TARGETED INACTIVATION OF PSAI REVEALS THE FUNCTION OF PSAI IN THE STRUCTURAL ORGANIZATION OF PSAL [J].
XU, Q ;
HOPPE, D ;
CHITNIS, VP ;
ODOM, WR ;
GUIKEMA, JA ;
CHITNIS, PR .
JOURNAL OF BIOLOGICAL CHEMISTRY, 1995, 270 (27) :16243-16250
[72]   Subcellular localization of the BtpA protein in the cyanobacterium Synechocystis sp. PCC 6803 [J].
Zak, E ;
Norling, B ;
Andersson, B ;
Pakrasi, HB .
EUROPEAN JOURNAL OF BIOCHEMISTRY, 1999, 261 (01) :311-316
[73]   The BtpA protein stabilizes the reaction center proteins of photosystem I in the cyanobacterium Synechocystis sp PCC 6803 at low temperature [J].
Zak, E ;
Pakrasi, HB .
PLANT PHYSIOLOGY, 2000, 123 (01) :215-222
[74]   Conformational changes in four regions of the Escherichia coli ArsA ATPase link ATP hydrolysis to ion translocation [J].
Zhou, TQ ;
Radaev, S ;
Rosen, BP ;
Gatti, DL .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2001, 276 (32) :30414-30422