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Titolo:
HUMAN RAD50 IS PHYSICALLY ASSOCIATED WITH HUMAN MRE11 - IDENTIFICATION OF A CONSERVED MULTIPROTEIN COMPLEX IMPLICATED IN RECOMBINATIONAL DNA-REPAIR
Autore:
DOLGANOV GM; MASER RS; NOVIKOV A; TOSTO L; CHONG S; BRESSAN DA; PETRINI JHJ;
Indirizzi:
GENELABS TECHNOL INC,HUMAN GENOME GRP,505 PENOBSCOT DR REDWOOD CITY CA 94063 UNIV WISCONSIN,SCH MED,GENET LAB MADISON WI 53706
Titolo Testata:
Molecular and cellular biology
fascicolo: 9, volume: 16, anno: 1996,
pagine: 4832 - 4841
SICI:
0270-7306(1996)16:9<4832:HRIPAW>2.0.ZU;2-V
Fonte:
ISI
Lingua:
ENG
Soggetto:
STRAND-BREAK REPAIR; IONIZING-RADIATION SENSITIVITY; MALIGNANT MYELOID DISORDERS; CHINESE-HAMSTER CELL; SACCHAROMYCES-CEREVISIAE; V(D)J RECOMBINATION; ESCHERICHIA-COLI; SCID MUTATION; HOMOLOGOUS RECOMBINATION; MEIOTIC RECOMBINATION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
91
Recensione:
Indirizzi per estratti:
Citazione:
G.M. Dolganov et al., "HUMAN RAD50 IS PHYSICALLY ASSOCIATED WITH HUMAN MRE11 - IDENTIFICATION OF A CONSERVED MULTIPROTEIN COMPLEX IMPLICATED IN RECOMBINATIONAL DNA-REPAIR", Molecular and cellular biology, 16(9), 1996, pp. 4832-4841

Abstract

In this report, we describe the identification and molecular characterization of a human RAD50 homolog, hRAD50. hRAD50 was included in a collection of cDNAs which were isolated by a direct cDNA selection strategy focused on the chromosomal interval spanning 5q23 to 5q31. Alterations of the 5q23-q31 interval are frequently observed in myelodysplasia and myeloid leukemia. This strategy was thus undertaken to create a detailed genetic map of that region. Saccharomyces cerevisiae RAD50 (ScRAD50) is one of three yeast RAD52 epistasis group members (ScRAD50, ScMRE11, and ScXRS2) in which mutations eliminate meiotic recombination but confer a hyperrecombinational phenotype in mitotic cells. The yeast Rad50, Mre11, and Xrs2 proteins appear to act in a multiprotein complex, consistent with the observation that the corresponding mutants confer essentially identical phenotypes. In this report, we demonstrate that the human Rad50 and Mre11 proteins are stably associated in a protein complex which may include three other proteins. hRAD50 is expressed in all tissues examined, but mRNA levels are significantly higherin the testis. Other human RAD52 epistasis group homologs exhibit this expression pattern, suggesting the involvement of human RAD52 epistasis group proteins in meiotic recombination. Human RAD52 epistasis group proteins are highly conserved and act in protein complexes that areanalogous to those of their yeast counterparts. These findings indicate that the function of the RAD52 epistasis group is conserved in human cells.

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Documento generato il 01/12/20 alle ore 08:02:27