Intrinsic membrane sector (Fo) of H+-ATPase (FoF1) from Escherichia coli. Mutations in the alpha subunit give Fo with impaired proton translocation and F1 binding.
Open Access
- 1 July 1988
- journal article
- research article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 263 (21) , 10056-10062
- https://doi.org/10.1016/s0021-9258(19)81476-x
Abstract
No abstract availableThis publication has 50 references indexed in Scilit:
- Improved M13 phage cloning vectors and host strains: nucleotide sequences of the M13mpl8 and pUC19 vectorsGene, 1985
- The UNC operon nucleotide sequence, regulation and structure of ATP-synthaseBiochimica et Biophysica Acta (BBA) - Reviews on Bioenergetics, 1984
- Two intervening sequences in the ATPase subunit 6 gene of Neurospora crassaJournal of Molecular Biology, 1984
- The proton conducting F0-part of bacterial ATP synthasesBiochimica et Biophysica Acta (BBA) - Reviews on Bioenergetics, 1984
- Secondary and tertiary structure of membrane proteins involved in proton translocationBiochimica et Biophysica Acta (BBA) - Reviews on Bioenergetics, 1983
- Complete sequence of bovine mitochondrial DNA conserved features of the mammalian mitochondrial genomeJournal of Molecular Biology, 1982
- Nucleotide sequence of the lexA gene of E. coliCell, 1981
- The proteolipid of a mutant ATPase from Escherichia coli defective in H+‐conduction contains a glycine instead of the carbodiimide‐reactive aspartyl residueFEBS Letters, 1980
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970
- Nonsense mutants and polarity in the Lac operon of Escherichia coliJournal of Molecular Biology, 1965