Structural analysis of a peptide synthetase gene required for ergopeptine production in the endophytic fungus Neotyphodium lolii

被引:8
作者
Damrongkool, P
Sedlock, AB
Young, CA
Johnson, RD
Goetz, KE
Scott, B
Schardl, CL
Panaccione, DG [1 ]
机构
[1] W Virginia Univ, Div Plant & Soil Sci, Morgantown, WV 26506 USA
[2] Massey Univ, Inst Mol Biosci, Palmerston North, New Zealand
[3] Univ Kentucky, Dept Plant Pathol, Lexington, KY 40546 USA
来源
DNA SEQUENCE | 2005年 / 16卷 / 05期
关键词
peptide synthetase; ergopeptine; adenylation domain; intron position; endophyte; ergovaline;
D O I
10.1080/10425170500273005
中图分类号
Q81 [生物工程学(生物技术)]; Q93 [微生物学];
学科分类号
071005 ; 0836 ; 090102 ; 100705 ;
摘要
Lysergyl peptide synthetase 1 catalyzes the assembly of toxic ergopeptines from activated D-lysergic acid and three amino acids. The gene encoding this enzyme in the endophytic fungus Neotyphodium lolii was analyzed and compared to a homologous gene from the ergot fungus Claviceps purpurea. Each gene contained two introns, which were found in the same relative position within two modules of the gene. The 5' ends of the two genes were unusually divergent. Signature sequences determining substrate specificity were similar in adenylation domains that recognized identical amino acids but differed within the adenylation domain for the amino acid that varies between the major ergopeptines of the two fungi. Homologues were detected in several related endophytic fungi; the tall fescue endophyte Neotyphodium coenophialum contained a divergent, second copy of the gene. Our results provide new information on the structure and distribution of this important peptide synthetase involved in ergot alkaloid biosynthesis.
引用
收藏
页码:379 / 385
页数:7
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