Structure of Tetrahymena CCTθ gene and its expression under colchicine treatment

被引:6
作者
Domingues, C
Soares, H
Rodrigues-Pousada, C
Cyrne, L
机构
[1] Inst Gulbenkian Ciencia, P-2781 Oeiras, Portugal
[2] Ecola Super Tecnol Saude Lisboa, P-1700 Lisbon, Portugal
[3] Univ Lisbon, Fac Ciencias, Dept Quim & Bioquim, P-1749016 Lisbon, Portugal
来源
BIOCHIMICA ET BIOPHYSICA ACTA-GENE STRUCTURE AND EXPRESSION | 1999年 / 1446卷 / 03期
关键词
CCT theta-chaperonin gene; ciliated protozoan; gene expression; colchicine;
D O I
10.1016/S0167-4781(99)00111-6
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
We report here the cloning and the characterization of the Tetrahymena pyriformis chaperonin-containing-TCP1 theta gene (TpCCT theta), an orthologue of the mouse chaperonin gene CCT theta. TpCCT theta gene is interrupted by eight introns, ranging in size between 91 and 419 nucleotides, and encodes a protein consisting of 540 amino acid residues (59.1 kDa), with a putative pI of 5.73. The amino acid sequence of TpCCT theta reveals 39.4-46.0% identity with the sequences of Candida albicans and mouse CCT theta subunits and 28.0-32.6% identity with the other TpCCT subunits known so far. We have studied the expression of this gene in exponentially growing Tetrahymena cells and in cells treated with colchicine for different times. The steady-state levels of CCT theta mRNA rapidly decrease in the first 30 min of colchicine treatment. Interestingly, treatment for subsequent 60 min gives expression levels higher than those found in exponentially growing cells. (C) 1999 Elsevier Science B.V. All rights reserved.
引用
收藏
页码:443 / 449
页数:7
相关论文
共 27 条
[1]   2 YEAST GENES WITH SIMILARITY TO TCP-1 ARE REQUIRED FOR MICROTUBULE AND ACTIN FUNCTION IN-VIVO [J].
CHEN, XY ;
SULLIVAN, DS ;
HUFFAKER, TC .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1994, 91 (19) :9111-9115
[2]   The Tetrahymena chaperonin subunit CCT eta gene is coexpressed with CCT gamma gene during cilia biogenesis and cell sexual reproduction [J].
Cyrne, L ;
Guerreiro, P ;
Cardoso, AC ;
RodriguesPousada, C ;
Soares, H .
FEBS LETTERS, 1996, 383 (03) :277-283
[3]  
Ellis R. John, 1996, P1
[4]   MOLECULAR CHAPERONES [J].
ELLIS, RJ ;
VANDERVIES, SM .
ANNUAL REVIEW OF BIOCHEMISTRY, 1991, 60 :321-347
[5]   FUNCTION IN PROTEIN FOLDING OF TRIC, A CYTOSOLIC RING COMPLEX CONTAINING TCP-1 AND STRUCTURALLY RELATED SUBUNITS [J].
FRYDMAN, J ;
NIMMESGERN, E ;
ERDJUMENTBROMAGE, H ;
WALL, JS ;
TEMPST, P ;
HARTL, FU .
EMBO JOURNAL, 1992, 11 (13) :4767-4778
[6]   2 COFACTORS AND CYTOPLASMIC CHAPERONIN ARE REQUIRED FOR THE FOLDING OF ALPHA-TUBULIN AND BETA-TUBULIN [J].
GAO, YI ;
VAINBERG, IE ;
CHOW, RL ;
COWAN, NJ .
MOLECULAR AND CELLULAR BIOLOGY, 1993, 13 (04) :2478-2485
[7]   A CYTOPLASMIC CHAPERONIN THAT CATALYZES BETA-ACTIN FOLDING [J].
GAO, YJ ;
THOMAS, JO ;
CHOW, RL ;
LEE, GH ;
COWAN, NJ .
CELL, 1992, 69 (06) :1043-1050
[8]   Molecular chaperones in cellular protein folding [J].
Hartl, FU .
NATURE, 1996, 381 (6583) :571-580
[9]   ANTIBODY CHARACTERIZATION OF 2 DISTINCT CONFORMATIONS OF THE CHAPERONIN-CONTAINING TCP-1 FROM MOUSE TESTIS [J].
HYNES, G ;
KUBOTA, H ;
WILLISON, KR .
FEBS LETTERS, 1995, 358 (02) :129-132
[10]  
KUBOTA H, 1995, EUR J BIOCHEM, V230, P3, DOI 10.1111/j.1432-1033.1995.0003i.x