MurAA, catalysing the first committed step in peptidoglycan biosynthesis, is a target of Clp-dependent proteolysis in Bacillus subtilis

被引:70
作者
Kock, H [1 ]
Gerth, U [1 ]
Hecker, M [1 ]
机构
[1] Ernst Moritz Arndt Univ Greifswald, Inst Mikrobiol & Mol Biol, D-17487 Greifswald, Germany
关键词
D O I
10.1046/j.1365-2958.2003.03875.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
The carboxyvinyl transfer from phosphoenolpyruvate to UDP-N-acetylglucosamine is the first committed step in the pathway of peptidoglycan formation. This crucial reaction for bacterial cell growth is catalysed by the MurA enzymes. Gram-negative bacteria carry one murA gene, whereas in a subgroup of Gram-positive bacteria two separate paralogues, MurAA and MurAB, exist. This study provides evidence that in the Gram-positive bacterium Bacillus subtilis, the MurAA protein is specifically degraded by the ClpCP protease. This Clp-dependent degradation is especially enhanced upon entry into stationary phase, thus ensuring an immediate growth arrest due to stalled murein biosynthesis. The MurAA protein can therefore be addressed as a target of Clp-dependent regulatory proteolysis such as the transcriptional regulators CtsR, ComK, Spx in B. subtilis, CtrA in Caulobacter crescentus or RpoS in Escherichia coli. Taking into account all other known regulatory targets of ATP-dependent proteases, MurAA of B. subtilis represents the first example of a metabolic enzyme which is a unique regulatory substrate of Clp-dependent proteolysis. Its function as a regulatory metabolic checkpoint resembles that of homoserine trans-succinylase (MetA) in E. coli which is similarly ATP-dependently degraded.
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页码:1087 / 1102
页数:16
相关论文
共 65 条
[1]   An Escherichia coli chromosomal ''addiction module'' regulated by 3',5'-bispyrophosphate: A model for programmed bacterial cell death [J].
Aizenman, E ;
EngelbergKulka, H ;
Glaser, G .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1996, 93 (12) :6059-6063
[2]   REQUIREMENTS FOR TRANSFORMATION IN BACILLUS SUBTILIS [J].
ANAGNOSTOPOULOS, C ;
SPIZIZEN, J .
JOURNAL OF BACTERIOLOGY, 1961, 81 (05) :741-&
[3]   Regulation of RpoS proteolysis in Escherichia coli:: The response regulator RssB is a recognition factor that interacts with the turnover element in RpoS [J].
Becker, G ;
Klauck, E ;
Hengge-Aronis, R .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1999, 96 (11) :6439-6444
[4]   GENE ENCODING THE SIGMA-37 SPECIES OF RNA-POLYMERASE SIGMA-FACTOR FROM BACILLUS-SUBTILIS [J].
BINNIE, C ;
LAMPE, M ;
LOSICK, R .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1986, 83 (16) :5943-5947
[5]   Control of methionine biosynthesis in Escherichia coli by proteolysis [J].
Biran, D ;
Gur, E ;
Gollan, L ;
Ron, EZ .
MOLECULAR MICROBIOLOGY, 2000, 37 (06) :1436-1443
[6]   DETECTION AND CHARACTERIZATION OF A PHOSPHOLACTOYL-ENZYME ADDUCT IN THE REACTION CATALYZED BY UDP-N-ACETYLGLUCOSAMINE ENOLPYRUVOYL TRANSFERASE, MURZ [J].
BROWN, ED ;
MARQUARDT, JL ;
LEE, JP ;
WALSH, CT ;
ANDERSON, KS .
BIOCHEMISTRY, 1994, 33 (35) :10638-10645
[7]  
Büttner K, 2001, ELECTROPHORESIS, V22, P2908, DOI 10.1002/1522-2683(200108)22:14<2908::AID-ELPS2908>3.0.CO
[8]  
2-M
[9]   ATP HYDROLYSIS-DEPENDENT PROTEASE ACTIVITY OF THE ION (CAPR) PROTEIN OF ESCHERICHIA-COLI K-12 [J].
CHARETTE, MF ;
HENDERSON, GW ;
MARKOVITZ, A .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA-BIOLOGICAL SCIENCES, 1981, 78 (08) :4728-4732
[10]   PHOSPHONOMYCIN - STRUCTURE AND SYNTHESIS [J].
CHRISTENSEN, BG ;
LEANZA, WJ ;
BEATTIE, TR ;
PATCHETT, AA ;
ARISON, BH ;
ORMOND, RE ;
KUEHL, FA ;
ALBERSSC.G ;
JARDETZKY, O .
SCIENCE, 1969, 166 (3901) :123-+