Linked Life Data

12053769

Source:http://linkedlifedata.com/resource/pubmed/id/12053769

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
2002-6-10
pubmed:abstractText
Proteosomes from human proerythroleukaemic cell line K562 are found to degrade high molecular weight cytoplasmic RNAs, particularly ribosomal and specific messenger RNA. This activity was observed to be endoribonucleotylic. The induction of differentiation by erythroid pathway in K562 cells invokes augmentation of endonuclease activity in proteasomes. The number of characteristics of this enzymatic activity was investigated. Specificity of endonuclease of these RNPs is shown to be Ca- and Mg-dependent. Dephosphorylation of protein subunits suppresses RNase activity of proteasomes. Endonuclease of proteasomes is thermolabile. The examined activity depends on the secondary structure of substrate RNA. Protein subunits are responsible for ribonuclease activity of proteasomes rather than for low molecular weight RNAs associated with the complex.
pubmed:language
rus
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0041-3771
pubmed:author
pubmed:issnType
Print
pubmed:volume
44
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
181-7
pubmed:dateRevised
2008-8-15
pubmed:meshHeading
pubmed:year
2002
pubmed:articleTitle
[Characteristics of endoribonuclease activity of proteasomes from K562 cells. I. Dependence of RNAase activity of proteasome and alph-RNP on conditions of endonucleolysis reaction].
pubmed:affiliation
Institute of Cytology RAS, St. Petersburg. agm@mail.cytspb.rssi.ru
pubmed:publicationType
Journal Article, English Abstract