Literature DB >> 8422943

N-terminal amino acid sequences of the subunits of the Na(+)-translocating F1F0 ATPase from Propionigenium modestum.

U Gerike1, P Dimroth.   

Abstract

We report here the N-terminal protein sequences of the subunits of the ATPase from Propionigenium modestum. Subunits c, b, delta, alpha and beta start with an N-terminal methionine residue, the gamma and epsilon subunits have an alanine N-terminus, from which N-formylmethionine was hydrolyzed by posttranslational modification, and subunit a contains a blocked N-terminus. Each of the N-terminal sequences exactly matches a portion of the DNA sequence in the gene encoding the respective subunit protein on the unc operon. Thus, the exact translational start for each subunit protein can be identified and the primary structures of the protein transcripts can be clearly defined. Based on these data the putative size of the open reading frame that was envisaged from the DNA sequence had to be revised for the alpha and delta subunits.

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Year:  1993        PMID: 8422943     DOI: 10.1016/0014-5793(93)81742-i

Source DB:  PubMed          Journal:  FEBS Lett        ISSN: 0014-5793            Impact factor:   4.124


  3 in total

1.  SpyA is a membrane-bound ADP-ribosyltransferase of Streptococcus pyogenes which modifies a streptococcal peptide, SpyB.

Authors:  Natalia Korotkova; Jessica S Hoff; Devon M Becker; John Kyle Heggen Quinn; Laura M Icenogle; Steve L Moseley
Journal:  Mol Microbiol       Date:  2012-01-30       Impact factor: 3.501

2.  Expression of subunits a and c of the sodium-dependent ATPase of Propionigenium modestum in Escherichia coli.

Authors:  U Gerike; P Dimroth
Journal:  Arch Microbiol       Date:  1994       Impact factor: 2.552

Review 3.  Bacterial sodium ion-coupled energetics.

Authors:  P Dimroth
Journal:  Antonie Van Leeuwenhoek       Date:  1994       Impact factor: 2.271

  3 in total

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