Linked Life Data

6220006

Source:http://linkedlifedata.com/resource/pubmed/id/6220006

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
7
pubmed:dateCreated
1983-5-5
pubmed:abstractText
The pattern and sites of phosphorylation of high mobility group (HMG) chromosomal proteins in HeLa cells labeled in vivo with [32P]orthophosphate have been compared with those of isolated HeLa HMG protein labeled in vitro by purified protein kinase enzymes. In synchronized HeLa cells there is phosphorylation of two HMG proteins designated hHMG 14 alpha 1 and alpha 2. hHMG 14 alpha 1 and alpha 2 are phosphorylated in a single identical tryptic phosphopeptide which runs toward the anode with electrophoresis at pH 4.7. The specific activity of phosphorylation at this site increased 2.5-fold in both hHMG 14 alpha 1 and alpha 2 in metaphase compared to interphase cultures. In vitro only casein kinase II specifically catalyzed phosphorylation of hHMG 14 alpha 1 and alpha 2 among a mixture of hHMG proteins; phosphorylation occurred at the site which was phosphorylated in vivo. The site of phosphorylation catalyzed by casein kinase II is distinct from sites in HMG proteins phosphorylated by cyclic nucleotide-dependent protein kinases or by casein kinase I. Casein kinase I specifically catalyzed phosphorylation of histone H1. These results indicate that casein kinase II is the enzyme which catalyzes the major phosphorylation of hHMG protein which occurs in vivo.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
10
pubmed:volume
258
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
4440-6
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed:year
1983
pubmed:articleTitle
Identity of the in vivo phosphorylation site in high mobility group 14 protein in HeLa cells with the site phosphorylated by casein kinase II in vitro.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.