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Titolo:
Sequence and expression of the SerJ immobilization antigen gene of Tetrahymena thermophila regulated by dominant epistasis
Autore:
Doerder, FP;
Indirizzi:
Cleveland State Univ, Dept Biol Geol & Environm Sci, Cleveland, OH 44115 USA Cleveland State Univ Cleveland OH USA 44115 Sci, Cleveland, OH 44115 USA
Titolo Testata:
GENE
fascicolo: 2, volume: 257, anno: 2000,
pagine: 319 - 326
SICI:
0378-1119(20001031)257:2<319:SAEOTS>2.0.ZU;2-J
Fonte:
ISI
Lingua:
ENG
Soggetto:
SURFACE PROTEIN GENE; PARAMECIUM-TETRAURELIA; MOLECULAR CHARACTERIZATION; I-ANTIGENS; CODON USAGE; PRIMAURELIA; PERIODICITY; SUBFAMILY; ALLELES;
Keywords:
codon usage; cysteine periodicity; GPI-linked protein; mRNA stability; variable surface protein;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
35
Recensione:
Indirizzi per estratti:
Indirizzo: Doerder, FP Cleveland State Univ, Dept Biol Geol & Environm Sci, Cleveland, OH 44115 USA Cleveland State Univ Cleveland OH USA 44115 and, OH 44115 USA
Citazione:
F.P. Doerder, "Sequence and expression of the SerJ immobilization antigen gene of Tetrahymena thermophila regulated by dominant epistasis", GENE, 257(2), 2000, pp. 319-326

Abstract

In ciliates, variable surface protein genes encoding the immobilization antigen (-ag) are expressed under different environmental conditions, including temperature and salt stress. These i-ags are GPI-linked and coat the entire external surface of the cell, including the cilia. In Tetrahymena thermophila-ag in natural isolates is the result of dominant epistasis masking the expression of the H i-ag ordinarily expressed at 20-36 degreesC. This report describes the expression and sequence of the Ser-ag. J is present on the cell surface up to 38 degreesC; above 38 degreesC SerSeranked by an A-rich 5' UTR and a 3' UTR containing putative mRNA destabilization motifs. Theencoded J polypeptide consists of 438 amino acids and is rich in alanine, cysteine, serine and threonine. The N- and resemble signal peptide and GPI-anchor addition sites, respectively. The majority of the molecule consists of four imperfect repeats with 10 periodic cysteines per repeat in the pattern CX6CX2CX21CX4CX13-15CX2CX18CX3CX11CX9-10. Although H i-ags encoded by paralogous SerH genes have 3.5 imperfect repeats with eight periodic cysteines per repeat, J nevertheless resembles H with respect to amino acid composition, codon usage, N- and C-termini, the arrangement of the cysteine periods, and regulation by mRNA stability. However, despite these similarities and epistasis, the evolutionary relationship between SerH and SerJ is unclear. (C) 2000 Elsevier Science B.V. All rights reserved.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 04/07/20 alle ore 14:46:55