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

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1993年 / 197卷 / 02期

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

页码：973 / 977

页数：5

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