Temperature-sensitive mutations at the carboxy terminus of the alpha subunit of the Escherichia coli F1F0 ATP synthase.
AUTOR(ES)
Vik, S B
RESUMO
Mutations were constructed in the a subunit of the F1F0 ATP synthase from Escherichia coli. Truncated forms of this subunit showed a temperature sensitivity phenotype. We conclude that the carboxy terminus of the a subunit is not involved directly with proton translocation but that it has an important structural role.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=208122Documentos Relacionados
- Mutations in the delta subunit influence the assembly of F1F0 ATP synthase in Escherichia coli.
- Construction and plasmid-borne complementation of strains lacking the epsilon subunit of the Escherichia coli F1F0 ATP synthase.
- Mutations at Glu-32 and His-39 in the epsilon subunit of the Escherichia coli F1F0 ATP synthase affect its inhibitory properties.
- Aqueous Accessibility to the Transmembrane Regions of Subunit c of the Escherichia coli F1F0 ATP Synthase*
- Isolation and characterization of an Escherichia coli mutant having temperature-sensitive farnesyl diphosphate synthase.
