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Titolo:
CLONING OF THE GENE ENCODING PEPTIDE-BINDING PROTEIN-74 SHOWS THAT ITIS A NEW MEMBER OF THE HEAT-SHOCK PROTEIN-70 FAMILY
Autore:
DOMANICO SZ; DENAGEL DC; DAHLSEID JN; GREEN JM; PIERCE SK;
Indirizzi:
NORTHWESTERN UNIV,DEPT BIOCHEM MOLEC BIOL & CELL BIOL EVANSTON IL 60208 NORTHWESTERN UNIV,DEPT BIOCHEM MOLEC BIOL & CELL BIOL EVANSTON IL 60208
Titolo Testata:
Molecular and cellular biology
fascicolo: 6, volume: 13, anno: 1993,
pagine: 3598 - 3610
SICI:
0270-7306(1993)13:6<3598:COTGEP>2.0.ZU;2-7
Fonte:
ISI
Lingua:
ENG
Soggetto:
ANTIGEN-PRESENTATION; MESSENGER-RNA; CELLS; IDENTIFICATION; PLAYS;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
40
Recensione:
Indirizzi per estratti:
Citazione:
S.Z. Domanico et al., "CLONING OF THE GENE ENCODING PEPTIDE-BINDING PROTEIN-74 SHOWS THAT ITIS A NEW MEMBER OF THE HEAT-SHOCK PROTEIN-70 FAMILY", Molecular and cellular biology, 13(6), 1993, pp. 3598-3610

Abstract

We have previously described peptide-binding proteins of 72 and 74 kDa (PBP72/74), which have been implicated as playing a role in antigen processing and are serologically related to the 70-kDa heat shock protein (hsp70) family. Here we report the cloning and sequencing of the cDNA encoding PBP74 in mice and in humans, accomplished by using amino acid sequence information obtained from the purified protein. We show that PBP74 is highly homologous to members of the hsp70 family but, significantly, is not identical to any known member of this family. Inspection of the cDNA nucleotide sequence indicates that it encodes a 46-residue N-terminal peptide which is not present in the mature protein. Transcription and translation in vitro of the PBP74 cDNA verified that it encodes a form of PBP74 which is larger than the mature protein. The presequence does not conform to known motifs for organelle-targeting sequences, and at present, its function is not known. By confocal microscopy, PBP74 was localized to cytoplasmic vesicles but not to the nucleus, mitochondria, or plasma membrane by using antibodies specificfor the N-terminal 16 residues of PBP74. By RNA filter hybridization analysis, PBP74 mRNAs are detected in all cell types tested. Exposure of cells to heat shock does not result in an increase in the mRNA levels of PBP74, unlike the dramatic increase observed for the stress-inducible hsp70 mRNA. Thus, PBP74 appears to be a constitutive, new memberof the hsp70 family.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 11/07/20 alle ore 03:57:22