Sec-independent protein translocation by the maize Hcf106 protein

被引:217
|
作者
Settles, AM
Yonetani, A
Baron, A
Bush, DR
Cline, K
Martienssen, R
机构
[1] COLD SPRING HARBOR LAB,COLD SPRING HARBOR,NY 11724
[2] EMORY UNIV,SCH MED,DEPT PSYCHIAT & BEHAV SCI,ATLANTA,GA 30322
[3] UNIV FLORIDA,DEPT HORT SCI,GAINESVILLE,FL 32611
[4] USDA ARS,PHOTOSYNTHESIS RES UNIT,URBANA,IL 61801
[5] UNIV ILLINOIS,DEPT PLANT BIOL,URBANA,IL 61801
关键词
D O I
10.1126/science.278.5342.1467
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
The bacterial Sec and signal recognition particle (ffh-dependent) protein translocation mechanisms are conserved between prokaryotes and higher plant chloroplasts. A third translocation mechanism in chloroplasts [the proton concentration difference (Delta pH) pathway] was previously thought to be unique. The hcf106 mutation of maize disrupts the localization of proteins transported through this Delta pH pathway in isolated chloroplasts. The Hcf106 gene encodes a receptor-like thylakoid membrane protein, which shows homology to open reading frames from all completely sequenced bacterial genomes, which suggests that the Delta pH pathway has been conserved since the endosymbiotic origin of chloroplasts. Thus, the third protein translocation pathway, of which HCF106 is a component, is found in both bacteria and plants.
引用
收藏
页码:1467 / 1470
页数:4
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