Role of the N-terminal signal peptide in the membrane insertion of Aquifex aeolicus F1F0 ATP synthase c-subunit.
FEBS J
; 280(14): 3425-35, 2013 Jul.
Article
em En
| MEDLINE
| ID: mdl-23663226
ABSTRACT
Rotary ATPases are membrane protein complexes that couple ATP hydrolysis to ion translocation across the membrane. Overall, they are evolutionarily well conserved, but the N-terminal segments of their rotary subunits (c-subunits) possess different lengths and levels of hydrophobicity across species. By analyzing the N-terminal variability, we distinguish four phylogenetic groups of c-subunits (groups 1-4). We characterize a member of group 2, the c-subunit from Aquifex aeolicus F1F0 ATP synthase, both in native cells and in a heterologous expression system. We demonstrate that its N-terminal segment forms a signal peptide with signal recognition particle (SRP) recognition features and is obligatorily required for membrane insertion. Based on our study and on previous characterizations of c-subunits from other organisms, we propose that c-subunits follow different membrane insertion pathways.
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MEDLINE
Assunto principal:
Proteínas de Bactérias
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Sinais Direcionadores de Proteínas
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ATPases Translocadoras de Prótons
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Subunidades Proteicas
Idioma:
En
Ano de publicação:
2013
Tipo de documento:
Article