Transcription attenuation

被引:68
作者
Gollnick, P [1 ]
Babitzke, P
机构
[1] SUNY Buffalo, Dept Biol Sci, Buffalo, NY 14260 USA
[2] Penn State Univ, Dept Biochem & Mol Biol, University Pk, PA 16802 USA
来源
BIOCHIMICA ET BIOPHYSICA ACTA-GENE STRUCTURE AND EXPRESSION | 2002年 / 1577卷 / 02期
关键词
attenuation; antitermination; gene regulation; transcriptional control; RNA-binding protein;
D O I
10.1016/S0167-4781(02)00455-4
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
In this review, we describe a variety of mechanisms that bacteria use to regulate transcription elongation in order to control gene expression in response to changes in their environment. Together, these mechanisms are known as attenuation and antitermination, and both involve controlling the formation of a transcription terminator structure in the RNA transcript prior to a structural gene or operon. We examine attenuation and antitermination from the point of view of the different biomolecules that are used to influence the RNA structure. Attenuation of many amino acid biosynthetic operons, particularly in enteric bacteria, is controlled by ribosomes translating leader peptides, RNA-binding proteins regulate attenuation, particularly in grain-positive bacteria such as Bacillus subtilis. Transfer RNA is also used to bind to leader RNAs and influence transcription antitermination in a large number of amino acyl tRNA synthetase genes and several biosynthetic genes in gram-positive bacteria. Finally, antisense RNA is involved in mediating transcription attenuation to control copy number of several plasmids. (C) 2002 Elsevier Science B.V. All rights reserved.
引用
收藏
页码:240 / 250
页数:11
相关论文
共 91 条
[1]   The lac operon of Lactobacillus casei contains lacT, a gene coding for a protein of the BglG family of transcriptional antiterminators [J].
Alpert, CA ;
Siebers, U .
JOURNAL OF BACTERIOLOGY, 1997, 179 (05) :1555-1562
[2]  
AMSTERCHODER O, 1990, J CELL BIOL, V51, P83
[3]  
[Anonymous], 1996, ESCHERICHIA COLI SAL
[4]   Structure of the trp RNA-binding attenuation protein, TRAP, bound to RNA [J].
Antson, AA ;
Dodson, EJ ;
Dodson, G ;
Greaves, RB ;
Chen, XP ;
Gollnick, P .
NATURE, 1999, 401 (6750) :235-242
[5]   THE STRUCTURE OF TRP RNA-BINDING ATTENUATION PROTEIN [J].
ANTSON, AA ;
OTRIDGE, J ;
BRZOZOWSKI, AM ;
DODSON, EJ ;
DODSON, GG ;
WILSON, KS ;
SMITH, TM ;
YANG, M ;
KURECKI, T ;
GOLLNICK, P .
NATURE, 1995, 374 (6524) :693-700
[6]   In vitro reconstitution of transcriptional antitermination by the SacT and SacY proteins of Bacillus subtilis [J].
Arnaud, M ;
Debarbouille, M ;
Rapoport, G ;
Saier, MH ;
Reizer, J .
JOURNAL OF BIOLOGICAL CHEMISTRY, 1996, 271 (31) :18966-18972
[7]  
Artz S. W., 1983, AMINO ACIDS BIOSYNTH, P379
[8]   Interaction of the trp RNA-binding attenuation protein (TRAP) of Bacillus subtilis with RNA: Effects of the number of GAG repeats, the nucleotides separating adjacent repeats, and RNA secondary structure [J].
Babitzke, P ;
Yealy, J ;
Campanelli, D .
JOURNAL OF BACTERIOLOGY, 1996, 178 (17) :5159-5163
[9]  
BABITZKE P, 1994, J BIOL CHEM, V269, P16597
[10]   Regulation of tryptophan biosynthesis: Trp-ing the TRAP or how Bacillus subtilis reinvented the wheel [J].
Babitzke, P .
MOLECULAR MICROBIOLOGY, 1997, 26 (01) :1-9