Linked Life Data

7556077

Source:http://linkedlifedata.com/resource/pubmed/id/7556077

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
17
pubmed:dateCreated
1995-10-27
pubmed:databankReference
pubmed:abstractText
Accumulation of globin mRNAs during erythroid differentiation is dependent on their extraordinary stability. The longevity of human alpha-globin mRNA is associated with a ribonucleoprotein complex (alpha-complex) formed on the 3' untranslated region (3'UTR). One or more of the proteins within this alpha-complex contain strong polycytosine [poly(C)] binding (alpha PCB) activity. In the present report we purify alpha PCB activity from human erythroid K562 cells. Although not able to bind the alpha-globin 3'UTR directly, alpha PCB activity is sufficient to complement alpha-complex formation in a cytosolic extract depleted of poly(C) binding activity. Peptide microsequencing demonstrates that alpha PCB activity contains two structurally related poly(C) binding proteins. These two proteins, alpha-complex protein (alpha CP)-1 and -2, have an overall structural identity of 80% and contain three repeats of the K homology (KH) domain which is found in a subset of RNA binding proteins. Epitope-tagged recombinant alpha CP-1 and alpha CP-2 expressed in cells are each incorporated into the alpha-complex. We conclude that alpha CP-1 and alpha CP-2, members of the KH domain RNA binding protein family, are involved in formation of a sequence-specific alpha-globin mRNP complex associated with alpha-globin mRNA stability. As such this represents the first example of a specific function for this class of proteins and suggests potential roles for other members of this protein family.
pubmed:grant
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/7556077-1353951, http://linkedlifedata.com/resource/pubmed/commentcorrection/7556077-1374686, http://linkedlifedata.com/resource/pubmed/commentcorrection/7556077-1485969, http://linkedlifedata.com/resource/pubmed/commentcorrection/7556077-1628625, http://linkedlifedata.com/resource/pubmed/commentcorrection/7556077-1710175, http://linkedlifedata.com/resource/pubmed/commentcorrection/7556077-1712670, http://linkedlifedata.com/resource/pubmed/commentcorrection/7556077-1716386, http://linkedlifedata.com/resource/pubmed/commentcorrection/7556077-1729596, http://linkedlifedata.com/resource/pubmed/commentcorrection/7556077-1802106, http://linkedlifedata.com/resource/pubmed/commentcorrection/7556077-2088178, http://linkedlifedata.com/resource/pubmed/commentcorrection/7556077-2231712, http://linkedlifedata.com/resource/pubmed/commentcorrection/7556077-2284008, http://linkedlifedata.com/resource/pubmed/commentcorrection/7556077-2699473, http://linkedlifedata.com/resource/pubmed/commentcorrection/7556077-3915782, http://linkedlifedata.com/resource/pubmed/commentcorrection/7556077-4101431, http://linkedlifedata.com/resource/pubmed/commentcorrection/7556077-4944483, http://linkedlifedata.com/resource/pubmed/commentcorrection/7556077-557727, http://linkedlifedata.com/resource/pubmed/commentcorrection/7556077-6894931, http://linkedlifedata.com/resource/pubmed/commentcorrection/7556077-6937265, http://linkedlifedata.com/resource/pubmed/commentcorrection/7556077-7104225, http://linkedlifedata.com/resource/pubmed/commentcorrection/7556077-7534458, http://linkedlifedata.com/resource/pubmed/commentcorrection/7556077-7687524, http://linkedlifedata.com/resource/pubmed/commentcorrection/7556077-7688265, http://linkedlifedata.com/resource/pubmed/commentcorrection/7556077-7688664, http://linkedlifedata.com/resource/pubmed/commentcorrection/7556077-7692601, http://linkedlifedata.com/resource/pubmed/commentcorrection/7556077-7739530, http://linkedlifedata.com/resource/pubmed/commentcorrection/7556077-7828735, http://linkedlifedata.com/resource/pubmed/commentcorrection/7556077-7862166, http://linkedlifedata.com/resource/pubmed/commentcorrection/7556077-7969150, http://linkedlifedata.com/resource/pubmed/commentcorrection/7556077-8036511, http://linkedlifedata.com/resource/pubmed/commentcorrection/7556077-8152927, http://linkedlifedata.com/resource/pubmed/commentcorrection/7556077-8156595, http://linkedlifedata.com/resource/pubmed/commentcorrection/7556077-8208614, http://linkedlifedata.com/resource/pubmed/commentcorrection/7556077-8318535, http://linkedlifedata.com/resource/pubmed/commentcorrection/7556077-8352591, http://linkedlifedata.com/resource/pubmed/commentcorrection/7556077-8367306, http://linkedlifedata.com/resource/pubmed/commentcorrection/7556077-8370540, http://linkedlifedata.com/resource/pubmed/commentcorrection/7556077-8380757, http://linkedlifedata.com/resource/pubmed/commentcorrection/7556077-8405383, http://linkedlifedata.com/resource/pubmed/commentcorrection/7556077-8464704, http://linkedlifedata.com/resource/pubmed/commentcorrection/7556077-8490650, http://linkedlifedata.com/resource/pubmed/commentcorrection/7556077-8500177, http://linkedlifedata.com/resource/pubmed/commentcorrection/7556077-949743
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0261-4189
pubmed:author
pubmed:issnType
Print
pubmed:day
1
pubmed:volume
14
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
4357-64
pubmed:dateRevised
2009-11-18
pubmed:meshHeading
pubmed:year
1995
pubmed:articleTitle
Identification of two KH domain proteins in the alpha-globin mRNP stability complex.
pubmed:affiliation
Howard Hughes Medical Institute, Department of Genetics, Philadelphia 19104-6145, USA.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't