Diversity and evolution of protein translocation.
Cells need to translocate proteins into and across hydrophobic membranes in order to interact with the extracellular environment. Although a subset of proteins are thought to spontaneously insert into lipid bilayers, translocation of most transported proteins requires additional cellular components. Such components catalyze efficient lateral transport into or across cellular membranes in prokaryotes and eukaryotes. These include, among others, the conserved YidC/Oxa1/Alb3 proteins as well as components of the Sec and the Tat pathways. Our current knowledge of the function and distribution of these components and their corresponding pathways in organisms of the three domains of life is reviewed. On the basis of this information, the evolution of protein translocation is discussed.
Pohlschröder
Mechthild
M
Department of Biology, University of Pennsylvania, Philadelphia, Pennsylvania 19104, USA. pohlschr@sas.upenn.edu
Hartmann
Enno
E
Hand
Nicholas J
NJ
Dilks
Kieran
K
Haddad
Alex
A
D000251:Adenosine Triphosphatases / Q000235:genetics; D000818:Animals; D001105:Archaea / Q000235:genetics*; D001419:Bacteria / Q000235:genetics*; D001426:Bacterial Proteins / Q000235:genetics; D029968:Escherichia coli Proteins / Q000235:genetics; D005057:Eukaryotic Cells; D019143:Evolution, Molecular; D014644:Genetic Variation; D006801:Humans; D026901:Membrane Transport Proteins / Q000235:genetics; D021381:Protein Transport / Q000235:genetics*; D000069816:SEC Translocation Channels; D000081416:SecA Proteins; D018271:Signal Recognition Particle / Q000235:genetics
D001426:Bacterial Proteins; D029968:Escherichia coli Proteins; D026901:Membrane Transport Proteins; D000069816:SEC Translocation Channels; D018271:Signal Recognition Particle; C412443:YIDC protein, E coli; C408585:twin-arginine translocase complex, E coli; D000251:Adenosine Triphosphatases; D000081416:SecA Proteins