Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
44
pubmed:dateCreated
2003-11-4
pubmed:abstractText
SR protein kinases (SRPKs) regulate the temporal and cell-specific selection of alternative splice sites. These enzymes are highly unique members of the protein kinase family. SRPKs contain a large domain insert (approximately 200 residues) within the kinase core, do not require phosphorylation for regulation, have an extended helix insert near the nucleotide pocket, and possess unusual substrate specificity determinants. The yeast SRPK, Sky1p, rapidly phosphorylates its natural substrate Npl3 but binds ATP with a high K(m), suggesting that some of these distinctive structural features may be correlated with nucleotide binding [Aubol et al. (2002) Biochemistry 41, 10002-10009]. To address this issue, the nucleotide binding properties of Sky1p were studied using fluorescence spectroscopy. The affinities of several nucleotides (ATP, ADP, AMP, adenosine, and AMPPNP) to Sky1p and the prototype kinase, cAMP-dependent protein kinase, were compared in the absence and presence of the metal activator, Mg(2+), using a fluorescence-based displacement assay. The data indicate that Sky1p, unlike cAMP-dependent protein kinase, potently destabilizes the gamma phosphate of ATP. This novel finding suggests that rapid phosphoryl transfer may be facilitated by unique mechanisms in both protein kinases.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/3'-O-(N-methylanthraniloyl) ATP, http://linkedlifedata.com/resource/pubmed/chemical/3'-O-(N-methylanthraniloyl)adenosine..., http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Diphosphate, http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Triphosphate, http://linkedlifedata.com/resource/pubmed/chemical/Anthranilic Acids, http://linkedlifedata.com/resource/pubmed/chemical/Cyclic AMP-Dependent Protein Kinases, http://linkedlifedata.com/resource/pubmed/chemical/Magnesium, http://linkedlifedata.com/resource/pubmed/chemical/Protein-Serine-Threonine Kinases, http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins, http://linkedlifedata.com/resource/pubmed/chemical/SKY1 protein, S cerevisiae, http://linkedlifedata.com/resource/pubmed/chemical/Saccharomyces cerevisiae Proteins
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0006-2960
pubmed:author
pubmed:issnType
Print
pubmed:day
11
pubmed:volume
42
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
12813-20
pubmed:dateRevised
2007-11-15
pubmed:meshHeading
pubmed-meshheading:14596595-Adenosine Diphosphate, pubmed-meshheading:14596595-Adenosine Triphosphate, pubmed-meshheading:14596595-Anthranilic Acids, pubmed-meshheading:14596595-Binding Sites, pubmed-meshheading:14596595-Cyclic AMP-Dependent Protein Kinases, pubmed-meshheading:14596595-Electron Transport, pubmed-meshheading:14596595-Enzyme Stability, pubmed-meshheading:14596595-Magnesium, pubmed-meshheading:14596595-Mutagenesis, Insertional, pubmed-meshheading:14596595-Protein Structure, Tertiary, pubmed-meshheading:14596595-Protein-Serine-Threonine Kinases, pubmed-meshheading:14596595-Recombinant Proteins, pubmed-meshheading:14596595-Saccharomyces cerevisiae Proteins, pubmed-meshheading:14596595-Sequence Deletion, pubmed-meshheading:14596595-Spectrometry, Fluorescence, pubmed-meshheading:14596595-Substrate Specificity
pubmed:year
2003
pubmed:articleTitle
Novel destabilization of nucleotide binding by the gamma phosphate of ATP in the yeast SR protein kinase Sky1p.
pubmed:affiliation
Department of Chemistry and Biochemistry, University of California, San Diego, La Jolla, California 92093-0506, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, U.S. Gov't, Non-P.H.S.