Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
51
pubmed:dateCreated
2007-3-6
pubmed:abstractText
Alpha subunit of Escherichia coli ATP synthase was expressed with a C-terminal 6-His tag and purified. Pure alpha was monomeric, was competent in nucleotide binding, and had normal N-terminal sequence. In F1 subunit dissociation/reassociation experiments it supported full reconstitution of ATPase, and reassociated complexes were able to bind to F1-depleted membranes with restoration of ATP-driven proton pumping. Therefore interaction between the stator delta subunit and the N-terminal residue 1-22 region of alpha occurred normally when pure alpha was complexed with other F1 subunits. On the other hand, three different types of experiments showed that no interaction occurred between pure delta and isolated alpha subunit. Unlike in F1, the N-terminal region of isolated alpha was not susceptible to trypsin cleavage. Therefore, during assembly of ATP synthase, complexation of alpha subunit with other F1 subunits is prerequisite for delta subunit binding to the N-terminal region of alpha. We suggest that the N-terminal 1-22 residues of alpha are sequestered in isolated alpha until released by binding of beta to alpha subunit. This prevents 1/1 delta/alpha complexes from forming and provides a satisfactory explanation of the stoichiometry of one delta per three alpha seen in the F1 sector of ATP synthase, assuming that steric hindrance prevents binding of more than one delta to the alpha3/beta3 hexagon. The cytoplasmic fragment of the b subunit (bsol) did not bind to isolated alpha. It might also be that complexation of alpha with beta subunits is prerequisite for direct binding of stator b subunit to the F1-sector.
pubmed:grant
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/17176112-10521283, http://linkedlifedata.com/resource/pubmed/commentcorrection/17176112-10836500, http://linkedlifedata.com/resource/pubmed/commentcorrection/17176112-10838050, http://linkedlifedata.com/resource/pubmed/commentcorrection/17176112-11080505, http://linkedlifedata.com/resource/pubmed/commentcorrection/17176112-11864990, http://linkedlifedata.com/resource/pubmed/commentcorrection/17176112-11997128, http://linkedlifedata.com/resource/pubmed/commentcorrection/17176112-12556473, http://linkedlifedata.com/resource/pubmed/commentcorrection/17176112-12788493, http://linkedlifedata.com/resource/pubmed/commentcorrection/17176112-12950181, http://linkedlifedata.com/resource/pubmed/commentcorrection/17176112-13061491, http://linkedlifedata.com/resource/pubmed/commentcorrection/17176112-143953, http://linkedlifedata.com/resource/pubmed/commentcorrection/17176112-14722065, http://linkedlifedata.com/resource/pubmed/commentcorrection/17176112-14744151, http://linkedlifedata.com/resource/pubmed/commentcorrection/17176112-14749768, http://linkedlifedata.com/resource/pubmed/commentcorrection/17176112-147871, http://linkedlifedata.com/resource/pubmed/commentcorrection/17176112-15069069, http://linkedlifedata.com/resource/pubmed/commentcorrection/17176112-15263011, http://linkedlifedata.com/resource/pubmed/commentcorrection/17176112-1530942, http://linkedlifedata.com/resource/pubmed/commentcorrection/17176112-1532797, http://linkedlifedata.com/resource/pubmed/commentcorrection/17176112-16045926, http://linkedlifedata.com/resource/pubmed/commentcorrection/17176112-16085645, http://linkedlifedata.com/resource/pubmed/commentcorrection/17176112-16128580, http://linkedlifedata.com/resource/pubmed/commentcorrection/17176112-16697972, http://linkedlifedata.com/resource/pubmed/commentcorrection/17176112-16730323, http://linkedlifedata.com/resource/pubmed/commentcorrection/17176112-16880204, http://linkedlifedata.com/resource/pubmed/commentcorrection/17176112-2156822, http://linkedlifedata.com/resource/pubmed/commentcorrection/17176112-2840354, http://linkedlifedata.com/resource/pubmed/commentcorrection/17176112-2891693, http://linkedlifedata.com/resource/pubmed/commentcorrection/17176112-2895769, http://linkedlifedata.com/resource/pubmed/commentcorrection/17176112-2903146, http://linkedlifedata.com/resource/pubmed/commentcorrection/17176112-5432063, http://linkedlifedata.com/resource/pubmed/commentcorrection/17176112-6193110, http://linkedlifedata.com/resource/pubmed/commentcorrection/17176112-6213603, http://linkedlifedata.com/resource/pubmed/commentcorrection/17176112-6218786, http://linkedlifedata.com/resource/pubmed/commentcorrection/17176112-6222731, http://linkedlifedata.com/resource/pubmed/commentcorrection/17176112-6238948, http://linkedlifedata.com/resource/pubmed/commentcorrection/17176112-6444218, http://linkedlifedata.com/resource/pubmed/commentcorrection/17176112-6446561, http://linkedlifedata.com/resource/pubmed/commentcorrection/17176112-6457026, http://linkedlifedata.com/resource/pubmed/commentcorrection/17176112-8051144, http://linkedlifedata.com/resource/pubmed/commentcorrection/17176112-8065448, http://linkedlifedata.com/resource/pubmed/commentcorrection/17176112-8113178, http://linkedlifedata.com/resource/pubmed/commentcorrection/17176112-8157656, http://linkedlifedata.com/resource/pubmed/commentcorrection/17176112-8412691, http://linkedlifedata.com/resource/pubmed/commentcorrection/17176112-9164460, http://linkedlifedata.com/resource/pubmed/commentcorrection/17176112-9480879, http://linkedlifedata.com/resource/pubmed/commentcorrection/17176112-9535839, http://linkedlifedata.com/resource/pubmed/commentcorrection/17176112-9614129
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Proton-Translocating..., http://linkedlifedata.com/resource/pubmed/chemical/Escherichia coli Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Mitochondrial Proton-Translocating..., http://linkedlifedata.com/resource/pubmed/chemical/Molecular Motor Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Peptide Fragments, http://linkedlifedata.com/resource/pubmed/chemical/Protein Subunits, http://linkedlifedata.com/resource/pubmed/chemical/Proton Pumps, http://linkedlifedata.com/resource/pubmed/chemical/Proton-Translocating ATPases, http://linkedlifedata.com/resource/pubmed/chemical/atpB protein, E coli, http://linkedlifedata.com/resource/pubmed/chemical/papE protein, E coli
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
1520-4995
pubmed:author
pubmed:issnType
Electronic
pubmed:day
26
pubmed:volume
45
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
15893-902
pubmed:dateRevised
2009-11-18
pubmed:meshHeading
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