Versatility of inner membrane protein biogenesis in Escherichia coli

被引：68

作者：

Fröderberg, L

Houben, E

Samuelson, JC

Chen, MY

Park, SK

Phillips, GJ

Dalbey, R

Luirink, J

de Gier, JWL ^{[1
]}

机构：

[1] Stockholm Univ, Arrhenius Labs, Dept Biochem & Biophys, SE-10691 Stockholm, Sweden

[2] BioCtr Amsterdam, Dept Microbiol, NL-1081 HV Amsterdam, Netherlands

[3] Ohio State Univ, Dept Chem, Columbus, OH 43210 USA

[4] Iowa State Univ, Dept Microbiol, Ames, IA 50011 USA

来源：

MOLECULAR MICROBIOLOGY | 2003年 / 47卷 / 04期

关键词：

D O I：

10.1046/j.1365-2958.2003.03346.x

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：

To further our understanding of inner membrane protein (IMP) biogenesis in Escherichia coli , we have accomplished the widest in vivo ioMP assembly screen so far. The biogenesis of a set of model IMPs covering most IMP structures possible has been studied in a variety of signal recognition particle (SRP), Sec and YidC mutant strains. We show that the assembly of the complete set of model IMPs is assisted (i.e. requires the aid of proteinaceous factors), and that the requirements for assembly of the model IMPs into the inner membrane differ significantly from each other. This indicates that IMP assembly is much more versatile than previously thought.

引用

页码：1015 / 1027

页数：13

共 75 条

[21] Assembly of a cytoplasmic membrane protein in Escherichia coli is dependent on the signal recognition particle [J].