THE SECD LOCUS OF ESCHERICHIA-COLI CODES FOR 2 MEMBRANE-PROTEINS REQUIRED FOR PROTEIN EXPORT

被引:151
作者
GARDEL, C [1 ]
JOHNSON, K [1 ]
JACQ, A [1 ]
BECKWITH, J [1 ]
机构
[1] UNIV PARIS 11,INST MICROBIOL,F-91405 ORSAY,FRANCE
关键词
membrane proteins; protein secretion; sec genes; TnphoA;
D O I
10.1002/j.1460-2075.1990.tb07519.x
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
Cold-sensitive mutations in the secD locus of Escherichia coli result in severe defects in protein export at the non-permissive temperature of 23°C. DNA sequence of a cloned fragment that includes the secD locus reveals open reading frames for seven polypeptide chains. Both deletions and TnphoA insertions in this clone have been used in maxicell and complementation studies to define the secD locus and its products. The secD mutations fall into two complementation groups, defining genes we have named secD and secF. These two genes comprise an operon, the first case of two genes involved in the export process being co-transcribed. The DNA sequence of the two genes along with alkaline phosphatase fusion analysis indicates that they code for integral proteins of the cytoplasmic membrane. We suggest that these two proteins may form a complex in the membrane which acts at late steps in the export process.
引用
收藏
页码:3209 / 3216
页数:8
相关论文
共 55 条
[1]   A GTP-BINDING PROTEIN OF ESCHERICHIA-COLI HAS HOMOLOGY TO YEAST RAS PROTEINS [J].
AHNN, J ;
MARCH, PE ;
TAKIFF, HE ;
INOUYE, M .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1986, 83 (23) :8849-8853
[2]   TOPOLOGY ANALYSIS OF THE SECY PROTEIN, AN INTEGRAL MEMBRANE-PROTEIN INVOLVED IN PROTEIN EXPORT IN ESCHERICHIA-COLI [J].
AKIYAMA, Y ;
ITO, K .
EMBO JOURNAL, 1987, 6 (11) :3465-3470
[3]   THE SECY MEMBRANE COMPONENT OF THE BACTERIAL PROTEIN EXPORT MACHINERY - ANALYSIS BY NEW ELECTROPHORETIC METHODS FOR INTEGRAL MEMBRANE-PROTEINS [J].
AKIYAMA, Y ;
ITO, K .
EMBO JOURNAL, 1985, 4 (12) :3351-3356
[4]   REGULATION OF ACETYLCHOLINE-RECEPTOR TRANSCRIPT EXPRESSION DURING DEVELOPMENT IN XENOPUS-LAEVIS [J].
BALDWIN, TJ ;
YOSHIHARA, CM ;
BLACKMER, K ;
KINTNER, CR ;
BURDEN, SJ .
JOURNAL OF CELL BIOLOGY, 1988, 106 (02) :469-478
[5]   MODEL FOR SIGNAL SEQUENCE RECOGNITION FROM AMINO-ACID-SEQUENCE OF 54K SUBUNIT OF SIGNAL RECOGNITION PARTICLE [J].
BERNSTEIN, HD ;
PORITZ, MA ;
STRUB, K ;
HOBEN, PJ ;
BRENNER, S ;
WALTER, P .
NATURE, 1989, 340 (6233) :482-486
[6]   SECA PROTEIN IS REQUIRED FOR SECRETORY PROTEIN TRANSLOCATION INTO ESCHERICHIA-COLI MEMBRANE-VESICLES [J].
CABELLI, RJ ;
CHEN, LL ;
TAI, PC ;
OLIVER, DB .
CELL, 1988, 55 (04) :683-692
[7]   INTERNAL DUPLICATION AND HOMOLOGY WITH BACTERIAL TRANSPORT PROTEINS IN THE MDR1 (P-GLYCOPROTEIN) GENE FROM MULTIDRUG-RESISTANT HUMAN-CELLS [J].
CHEN, CJ ;
CHIN, JE ;
UEDA, K ;
CLARK, DP ;
PASTAN, I ;
GOTTESMAN, MM ;
RONINSON, IB .
CELL, 1986, 47 (03) :381-389
[8]  
CHEN CM, 1986, J BIOL CHEM, V261, P5030
[9]   70K HEAT-SHOCK RELATED PROTEINS STIMULATE PROTEIN TRANSLOCATION INTO MICROSOMES [J].
CHIRICO, WJ ;
WATERS, MG ;
BLOBEL, G .
NATURE, 1988, 332 (6167) :805-810
[10]   THE ANTIFOLDING ACTIVITY OF SECB PROMOTES THE EXPORT OF THE ESCHERICHIA-COLI MALTOSE-BINDING PROTEIN [J].
COLLIER, DN ;
BANKAITIS, VA ;
WEISS, JB ;
BASSFORD, PJ .
CELL, 1988, 53 (02) :273-283