A novel plant peptidyl-prolyl-cis-trans-isomerase (PPIase): cDNA cloning, structural analysis, enzymatic activity and expression

被引：57
作者：
Blecher, O
Erel, N
Callebaut, I
Aviezer, K
Breiman, A
机构：
[1] TEL AVIV UNIV, GEORGE S WISE FAC LIFE SCI, DEPT BOT, IL-69978 TEL AVIV, ISRAEL
[2] UNIV PARIS 06, CNRS, LAB MINERAL CRISTALLOG, URA 09, F-75252 PARIS 05, FRANCE
[3] UNIV PARIS 07, CNRS, LAB MINERAL CRISTALLOG, URA 09, F-75252 PARIS 05, FRANCE
来源：
PLANT MOLECULAR BIOLOGY | 1996年 / 32卷 / 03期
关键词：
cDNA; expression; FKBP; PPIase; wheat;
D O I：
10.1007/BF00019101
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 novel cDNA encoding for a peptidyl-prolyl-cis-trans-isomerase (PPIase) belonging to the FK506-binding protein (FKBP) family was isolated from wheat. It contains an open reading frame of 559 amino acids and it represents the first plant FKBP-PPIase to be cloned. It possesses a unique sequence which is composed of three FKPB-like domains, in addition to a putative tetratricopeptide repeat (TPR) motif and a calmodulin-binding site. The recombinant FKBP-PPIase expressed in and purified from Escherichia coli exhibits PPIase activity that is efficiently inhibited by the immunosuppressive drugs FK506 and rapamycin. Northern blot analysis showed that wheat FKBP was found mainly in young tissues. Polyclonal antibodies revealed the presence of cross-reacting proteins in embryos, roots and shoots. The unique structural features, the enzymatic activity and the presence of putative isoforms in wheat tissues indicate the possibility of the involvement of wheat PPIase in essential biological functions, similar to other members of the FKBP gene family.
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收藏
页码：493 / 504
页数：12
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