Characterization of a Schistosoma mansoni gene encoding a homologue of the Y-box binding protein

被引:25
作者
Franco, GR
Garratt, RC
Tanaka, M
Simpson, AJG
Pena, SDJ
机构
[1] UNIV FED MINAS GERAIS,INST CIENCIAS BIOL,DEPT BIOQUIM & IMUNOL,BR-31270010 BELO HORIZONT,MG,BRAZIL
[2] UNIV FED SAO CARLOS,DEPT FIS & INFORMAT,BR-13560970 SAO CARLOS,SP,BRAZIL
[3] MINIST INT TRADE & IND,AGCY IND SCI & TECHNOL,NATL INST BIOSCI & HUMAN TECHNOL,TSUKUBA,IBARAKI 305,JAPAN
[4] INST LUDWIG PESQUISAS CANC,BR-01509010 SAO PAULO,BRAZIL
关键词
expressed sequence tag; cold-shock domain; computational modeling; RT-PCR;
D O I
10.1016/S0378-1119(97)00261-8
中图分类号
Q3 [遗传学];
学科分类号
071007 ; 090102 ;
摘要
We have cloned and characterized a Schistosoma mansoni cDNA encoding a basic protein homologous to the human Y-box binding protein 1 (YB-1). The 1.3-kb S. mansoni YB-1 transcript, which was shown to be expressed in various stages of the parasite life cycle, codes for a protein of 217 amino acids containing, towards its N-terminus, a nucleic acid binding motif, known as the cold-shock domain (CSD). This domain is 64% identical to the cold-shock domain of other members of the Y-box binding protein family and 43% identical to the cold-shock protein CspA of Escherichia coli. In S mansoni YB-1, the cold-shock domain possess some structural characteristics that permit dimer formation as occurs in the Bacillus subtilis cold-shock protein CspB. The C-terminal region of S. mansoni YB-1 differs from the other Y-box binding proteins because of the presence of tandem repeats of Arg and Gly, suggesting the formation of a fibroin-like beta-sandwich structure. This novel folding pattern for the C-terminus of S. mansoni YB-1 might suggest a distinct specific function for this protein in the parasite. (C) 1997 Elsevier Science B.V.
引用
收藏
页码:5 / 16
页数:12
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