Linked Life Data

8161217

Source:http://linkedlifedata.com/resource/pubmed/id/8161217

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1994-5-18
pubmed:abstractText
Irradiation of the F1-ATPase from Bacillus PS3 (TF1) in the presence of 134 microM 2-N3-[beta, gamma-32P]ATP plus Mg2+ for 90 min led to 95% inactivation of the ATPase activity which was accompanied by exclusive labeling of the beta subunit. The isolated alpha and beta subunits were also treated separately with 2-N3-[beta, gamma-32P]ATP under similar conditions. Fractionation of a tryptic digest of photolabeled TF1 by reversed-phase HPLC resolved a major and a minor radioactive peptide. Sequence analyses showed that the major peptide contained labeled Tyr-beta 364, whereas the minor one contained labeled Tyr-beta 341, residues known to be part of noncatalytic and catalytic sites, respectively. Two closely eluting radioactive peptides were obtained when a tryptic digest of the photolabeled, isolated beta subunit was fractionated by HPLC. Sequence analyses revealed that both contained labeled Tyr-beta 341. Fractionation of a tryptic digest of the photolabeled, isolated alpha subunit by HPLC resolved two peptides which contained the majority of the radioactivity incorporated. When subjected to eight cycles of automatic Edman degradation, one gave the sequence APGVXDR, corresponding to residues 133-139, in which X is a gap and corresponds to Met-alpha 137, which presumably is the derivatized residue. Only the first five cycles yielded phenylthiohydantoin derivatives when the other radioactive peptide derived from the alpha subunit was submitted to automatic Edman degradation which revealed the sequence APGVM, suggesting that Asp-alpha 138 is derivatized. The overall results suggest that the isolated beta subunit is a useful model for studying binding of nucleotides to catalytic sites, whereas the isolated alpha subunit may be of limited value in modeling interactions of nucleotides with noncatalytic sites.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0003-9861
pubmed:author
pubmed:issnType
Print
pubmed:volume
310
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
282-8
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1994
pubmed:articleTitle
Probing the specificity of nucleotide binding to the F1-ATPase from thermophilic Bacillus PS3 and its isolated alpha and beta subunits with 2-N3-[beta, gamma-32P]ATP.
pubmed:affiliation
Department of Chemistry, University of California at San Diego, La Jolla 92093-0601.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.