Bacillus subtilis antibiotics:: structures, syntheses and specific functions

被引:1206
作者
Stein, T [1 ]
机构
[1] Goethe Univ Frankfurt, Inst Mikrobiol, D-60439 Frankfurt, Germany
关键词
D O I
10.1111/j.1365-2958.2005.04587.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 endospore-forming rhizobacterium Bacillus subtilis - the model system for Gram-positive organisms, is able to produce more than two dozen antibiotics with an amazing variety of structures. The produced anti-microbial active compounds include predominantly peptides that are either ribosomally synthesized and post-translationally modified (lantibiotics and lantibiotic-like peptides) or non-ribosomally generated, as well as a couple of non-peptidic compounds such as polyketides, an aminosugar, and a phospholipid. Here I summarize the structures of all known B. subtilis antibiotics, their biochemistry and genetic analysis of their biosyntheses. An updated summary of well-studied antibiotic regulation pathways is given. Furthermore, current findings are resumed that show roles for distinct B. subtilis antibiotics beyond the 'pure' anti-microbial action: Non-ribosomally produced lipopeptides are involved in biofilm and swarming development, lantibiotics function as pheromones in quorum-sensing, and a 'killing factor' effectuates programmed cell death in sister cells. A discussion of how these antibiotics may contribute to the survival of B. subtilis in its natural environment is given.
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收藏
页码:845 / 857
页数:13
相关论文
共 108 条
[1]   Biocontrol of Bacillus subtilis against infection of Arabidopsis roots by Pseudomonas syringae is facilitated by biofilm formation and surfactin production [J].
Bais, HP ;
Fall, R ;
Vivanco, JM .
PLANT PHYSIOLOGY, 2004, 134 (01) :307-319
[2]   Structure of MrsD, an FAD-binding protein of the HFCD family [J].
Blaesse, M ;
Kupke, T ;
Huber, R ;
Steinbacher, S .
ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY, 2003, 59 :1414-1421
[3]   Genes involved in formation of structured multicellular communities by Bacillus subtilis [J].
Branda, SS ;
González-Pastor, JE ;
Dervyn, E ;
Ehrlich, SD ;
Losick, R ;
Kolter, R .
JOURNAL OF BACTERIOLOGY, 2004, 186 (12) :3970-3979
[4]   Fruiting body formation by Bacillus subtilis [J].
Branda, SS ;
González-Pastor, JE ;
Ben-Yehuda, S ;
Losick, R ;
Kolter, R .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2001, 98 (20) :11621-11626
[5]   Use of the cell wall precursor lipid II by a pore-forming peptide antibiotic [J].
Breukink, E ;
Wiedemann, I ;
van Kraaij, C ;
Kuipers, OP ;
Sahl, HG ;
de Kruijff, B .
SCIENCE, 1999, 286 (5448) :2361-2364
[6]   The lantibiotic mersacidin inhibits peptidoglycan biosynthesis at the level of transglycosylation [J].
Brotz, H ;
Bierbaum, G ;
Reynolds, PE ;
Sahl, HG .
EUROPEAN JOURNAL OF BIOCHEMISTRY, 1997, 246 (01) :193-199
[7]  
Budzikiewicz H, 1997, Z NATURFORSCH C, V52, P551
[8]   INDUCED BIOCHEMICAL MUTATIONS IN BACILLUS-SUBTILIS [J].
BURKHOLDER, PR ;
GILES, NH .
AMERICAN JOURNAL OF BOTANY, 1947, 34 (06) :345-348
[9]   Molecular mechanism of membrane permeabilization by the peptide antibiotic surfactin [J].
Carrillo, C ;
Teruel, JA ;
Aranda, FJ ;
Ortiz, A .
BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES, 2003, 1611 (1-2) :91-97
[10]   Activation of subtilin precursors by Bacillus subtilis extracellular serine proteases subtilisin (AprE), WprA, and Vpr [J].
Corvey, C ;
Stein, T ;
Düsterhus, S ;
Karas, M ;
Entian, KD .
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 2003, 304 (01) :48-54