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Titolo:
HOMODIMERIZATION OF THE HUMAN U1 SNRNP-SPECIFIC PROTEIN-C
Autore:
GUNNEWIEK JMTK; VANAARSSEN Y; WASSENAAR R; LEGRAIN P; VANVENROOIJ WJ; NELISSEN RLH;
Indirizzi:
UNIV NIJMEGEN,DEPT BIOCHEM,POB 9101 6500 HB NIJMEGEN NETHERLANDS INST PASTEUR,DEPT BIOTECHNOL F-75724 PARIS 15 FRANCE
Titolo Testata:
Nucleic acids research
fascicolo: 23, volume: 23, anno: 1995,
pagine: 4864 - 4871
SICI:
0305-1048(1995)23:23<4864:HOTHUS>2.0.ZU;2-Q
Fonte:
ISI
Lingua:
ENG
Soggetto:
T7 RNA-POLYMERASE; SMALL NUCLEAR-RNA; 5' SPLICE SITE; BINDING; IDENTIFICATION; EXPRESSION; INVITRO; AUTOANTIBODIES; PURIFICATION; SYSTEM;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
33
Recensione:
Indirizzi per estratti:
Citazione:
J.M.T.K. Gunnewiek et al., "HOMODIMERIZATION OF THE HUMAN U1 SNRNP-SPECIFIC PROTEIN-C", Nucleic acids research, 23(23), 1995, pp. 4864-4871

Abstract

The U1 snRNP-specific protein C contains an N-terminal zinc finger-like CH motif which is required for the binding of the U1C protein to the U1 snRNP particle, Recently a similar motif was reported to be essential for in vivo homodimerization of the yeast splicing factor PRP9. In the present study we demonstrate that the human U1C protein is able to form homodimers as well, U1C homodimers are found when (i) the human U1C protein is expressed in Escherichia coil, (ii) immunoprecipitations with anti-U1C antibodies are performed on in vitro translated U1C,and when (iii) the yeast two hybrid system is used. Analyses of mutant U1C proteins in an in vitro dimerization assay and the yeast two hybrid system revealed that amino acids within the CH motif, i.e. betweenpositions 22 and 30, are required for homodimerization.

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Documento generato il 04/12/20 alle ore 11:35:01