CDNA CLONING OF A PUTATIVE PROTOCHORADATE FK506-BINDING PROTEIN

被引:17
作者
PANCER, Z [1 ]
GERSHON, H [1 ]
RINKEVICH, B [1 ]
机构
[1] TECHNION ISRAEL INST TECHNOL,BRUCE RAPPAPORT FAC MED,DEPT IMMUNOL,IL-31096 HAIFA,ISRAEL
关键词
D O I
10.1006/bbrc.1993.2574
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
A tunicate (Botryllus schlosseri) cDNA library was screened with a microsatellite probe. Five positive clones were sequenced, each with a 5′ truncated microsatellite. One (Bs.6) revealed striking similarity to FK506 and rapamycin-binding proteins (FKBPs). Clone Bs.6 is 500 base pairs long and encodes for a putative protein of 134 amino acids. The predicted protein features the two FKBP-type peptidyl-prolyl cis-trans isomerase (PPIase) signatures and an endoplasmic reticulum retention signal. This protochordate protein is substantially similar to 12-13 kDa FKBPs, most remarkably to one of the receptors that had been proposed to mediate the immunosuppressive actions of FK506, the human FKBP-13 (62% amino acid identity and 74% similarity). © 1993 Academic Press. All rights reserved.
引用
收藏
页码:973 / 977
页数:5
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