Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1995-12-18
pubmed:databankReference
pubmed:abstractText
Three cDNA clones encoding isoforms of casein kinase I (CKI) were isolated from Arabidopsis thaliana. One full-length clone, designated CKI1, contained an open reading frame of 1371 bp encoding a protein of 51,949 D with an isoelectric point of 9.7. In addition to the highly conserved catalytic domain (of about 300 amino acids), the Arabidopsis CKI isoforms contain 150 to 180 amino acid carboxyl-terminal extensions, which show among themselves a lower level of sequence conservation. These extensions do not show any sequence similarity to nonplant CKI isoforms, such as rat testis CKI delta, which is their closest isolated homolog, or to yeast CKI isoforms. Three additional isoforms of Arabidopsis CKI were found in the data bases of expressed sequence tags and/or were isolated serendipitously in nonspecific screening procedures by others. One of them also shows a carboxyl-terminal extension, but of only 80 amino acids. Casein kinase activity was detected in the soluble fraction of Escherichia coli strains expressing the CKI1 protein. This activity showed the crucial properties of CKI, including the ability to phosphorylate the D4 peptide, a specific substrate of CKI, and inhibition by N-(2-aminoethyl)-5-chloroisoquinoline-8-sulfonamide, a specific CKI inhibitor. Like several recombinant CKI isoforms from yeast, CKI1 was able to phosphorylate tyrosine-containing acidic polymers.
pubmed:grant
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/7480353-1400350, http://linkedlifedata.com/resource/pubmed/commentcorrection/7480353-1495994, http://linkedlifedata.com/resource/pubmed/commentcorrection/7480353-1627830, http://linkedlifedata.com/resource/pubmed/commentcorrection/7480353-1650349, http://linkedlifedata.com/resource/pubmed/commentcorrection/7480353-1729698, http://linkedlifedata.com/resource/pubmed/commentcorrection/7480353-1835511, http://linkedlifedata.com/resource/pubmed/commentcorrection/7480353-1852075, http://linkedlifedata.com/resource/pubmed/commentcorrection/7480353-1995625, http://linkedlifedata.com/resource/pubmed/commentcorrection/7480353-1997039, http://linkedlifedata.com/resource/pubmed/commentcorrection/7480353-2117608, http://linkedlifedata.com/resource/pubmed/commentcorrection/7480353-2199796, http://linkedlifedata.com/resource/pubmed/commentcorrection/7480353-2925675, http://linkedlifedata.com/resource/pubmed/commentcorrection/7480353-3291115, http://linkedlifedata.com/resource/pubmed/commentcorrection/7480353-6937462, http://linkedlifedata.com/resource/pubmed/commentcorrection/7480353-7527390, http://linkedlifedata.com/resource/pubmed/commentcorrection/7480353-7696877, http://linkedlifedata.com/resource/pubmed/commentcorrection/7480353-7759525, http://linkedlifedata.com/resource/pubmed/commentcorrection/7480353-7803855, http://linkedlifedata.com/resource/pubmed/commentcorrection/7480353-7906398, http://linkedlifedata.com/resource/pubmed/commentcorrection/7480353-8074660, http://linkedlifedata.com/resource/pubmed/commentcorrection/7480353-8163505, http://linkedlifedata.com/resource/pubmed/commentcorrection/7480353-8292342, http://linkedlifedata.com/resource/pubmed/commentcorrection/7480353-8328968, http://linkedlifedata.com/resource/pubmed/commentcorrection/7480353-8380893, http://linkedlifedata.com/resource/pubmed/commentcorrection/7480353-8454611
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0032-0889
pubmed:author
pubmed:issnType
Print
pubmed:volume
109
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
687-96
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed-meshheading:7480353-Amino Acid Sequence, pubmed-meshheading:7480353-Animals, pubmed-meshheading:7480353-Arabidopsis, pubmed-meshheading:7480353-Base Sequence, pubmed-meshheading:7480353-Binding Sites, pubmed-meshheading:7480353-Casein Kinases, pubmed-meshheading:7480353-Cloning, Molecular, pubmed-meshheading:7480353-Conserved Sequence, pubmed-meshheading:7480353-Escherichia coli, pubmed-meshheading:7480353-Humans, pubmed-meshheading:7480353-Isoenzymes, pubmed-meshheading:7480353-Male, pubmed-meshheading:7480353-Molecular Sequence Data, pubmed-meshheading:7480353-Molecular Weight, pubmed-meshheading:7480353-Open Reading Frames, pubmed-meshheading:7480353-Phylogeny, pubmed-meshheading:7480353-Protein Kinases, pubmed-meshheading:7480353-RNA, Messenger, pubmed-meshheading:7480353-Rats, pubmed-meshheading:7480353-Recombinant Proteins, pubmed-meshheading:7480353-Restriction Mapping, pubmed-meshheading:7480353-Saccharomyces cerevisiae, pubmed-meshheading:7480353-Sequence Homology, Amino Acid, pubmed-meshheading:7480353-Testis
pubmed:year
1995
pubmed:articleTitle
Multiple isoforms of Arabidopsis casein kinase I combine conserved catalytic domains with variable carboxyl-terminal extensions.
pubmed:affiliation
Department of Biology, University of Pennsylvania, Philadelphia 19104, USA.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, U.S. Gov't, P.H.S., Research Support, U.S. Gov't, Non-P.H.S., Research Support, Non-U.S. Gov't