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Titolo:
Characterization of ostrich (Struthio camelus) beta-microseminoprotein (MSP): Identification of homologous sequences in EST databases and analysis oftheir evolution during speciation
Autore:
Lazure, C; Villemure, M; Gauthier, D; Naude, RJ; Mbikay, M;
Indirizzi:
Univ Montreal, Inst Rech Clin Montreal, Lab Struct & Metab Neuropeptides, Montreal, PQ H2W 1R7, Canada Univ Montreal Montreal PQ Canada H2W 1R7 es, Montreal, PQ H2W 1R7, Canada Univ Port Elizabeth, Dept Biochem & Microbiol, ZA-6000 Port Elizabeth, South Africa Univ Port Elizabeth Port Elizabeth South Africa ZA-6000 th, South Africa Univ Ottawa, Ottawa Hosp, Ottawa Hlth Res Inst, Ottawa, ON K1Y 4K9, CanadaUniv Ottawa Ottawa ON Canada K1Y 4K9 Res Inst, Ottawa, ON K1Y 4K9, Canada
Titolo Testata:
PROTEIN SCIENCE
fascicolo: 11, volume: 10, anno: 2001,
pagine: 2207 - 2218
SICI:
0961-8368(200111)10:11<2207:COO(CB>2.0.ZU;2-F
Fonte:
ISI
Lingua:
ENG
Soggetto:
PROSTATIC SECRETORY PROTEIN; HUMAN SEMINAL PLASMA; 94 AMINO-ACIDS; IMMUNOGLOBULIN BINDING-FACTOR; GENE-EXPRESSION ANALYSIS; MOLECULAR-CLONING; CELL-LINES; INHIBIN PEPTIDE; MESSENGER-RNA; PSP94;
Keywords:
microseminoprotein; prostate secretory protein; protein evolution-; Struthio camelus; protein sequencing; disulfide bonds;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
52
Recensione:
Indirizzi per estratti:
Indirizzo: Lazure, C Univ Montreal, Inst Rech Clin Montreal, Lab Struct & Metab Neuropeptides, 110 Pine Ave W, Montreal, PQ H2W 1R7, Canada Univ Montreal 110 Pine Ave W Montreal PQ Canada H2W 1R7 , Canada
Citazione:
C. Lazure et al., "Characterization of ostrich (Struthio camelus) beta-microseminoprotein (MSP): Identification of homologous sequences in EST databases and analysis oftheir evolution during speciation", PROTEIN SCI, 10(11), 2001, pp. 2207-2218

Abstract

beta -Microseminoprotein, alternatively called prostatic secretory proteinof 94 amino acids, is a hydrophilic, unglycosylated, small protein rich inconserved half-cystine residues. Originally found in human seminal plasma and prostatic fluids, its presence was later shown in numerous secretions and its homologs were described in many vertebrate species. These studies showed that this protein had rapidly evolved, but they failed to unambiguously identify its biological role. Here, we show that a protein isolated from ostrich pituitary gland is closely related to a similar one isolated from chicken ser-um and that the two are structurally related to the mammalian beta -microseminoprotein. The complete 90-amino acid sequence of the ostrich molecule was established through a combination of automated Edman degradation and matrix-assisted laser desorption ionization-time of flight (MALDI-TOF) mass spectrometric procedures, including postsource decay (PSD) and ladder sequencing analyses. This study documents for the first time that beta -microseminoprotein is present in aves. It is also the first report of a C-terminal amidated form for a member of this protein family and the first in which the disulfide linkages are established, Database searches using the herein-de scribed amino acid sequence allowed identification of related proteins in numerous species such as cow, African clawed frog, zebrafish, and Japanese flounder. These small proteins show a strikingly high rate of aminoacid substitutions, especially across phyla boundaries. Noticeably, no beta -microseminoprotein-related gene could be found in the recently completedfruit fly genome. indicating that if such a gene exists in arthropods, it must have extensively diverged from the vertebrate ones.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 04/12/20 alle ore 09:13:40