Nucleotide sequence and functional analysis of the luxE gene encoding acyl-protein synthetase of the lux operon from Photobacterium leiognathi

Biochemical and Biophysical Research Communications
J W LinS F Weng

Abstract

Nucleotide sequence of the luxE gene GenBank Accession No. U66407 from Photobacterium leiognathi PL741 has been determined, and the amino acid sequence of acyl-protein synthetase encoded by the luxE gene is deduced. Nucleotide sequence reveals that the luxE gene encodes acyl-protein synthetase, which is a component of the fatty acid reductase complex that is responsible for converting fatty acid to aldehyde as substrate in the luciferase-catalyzed bioluminescence reaction. The acyl-protein synthetase encoded by the luxE gene has a calculated M, 43,128 and comprises 373 amino acid residues. Alignment and comparison of acyl-protein synthetases from P. leiognathi, P. phosphoreum, Vibrio fischeri, V. harveyi and Xenorhabdus luminescens shows that they are homologous; there is 75.5% homologous (44.2% identity and 31.3% similarity) among these species. Functional analysis illustrates that the specific segment sequence lying before or in the luxE gene might from potential loops omega o omega e1, omega e2 as mRNA stability loop and/or for sub-regulation by alternative modulation in the lux operon. The gene order of the luxE gene in the lux and the lum operons is<--ter-lumQ-lumP-R&R-luxC-luxD-luxA-luxB -luxN-luxE-->(R&R: regulatory regi...Continue Reading

Citations

Dec 25, 2003·Antimicrobial Agents and Chemotherapy·Shu-Fen WengYi-Hsiung Tseng
Dec 15, 2004·Biochemical and Biophysical Research Communications·Juey-Wen LinYi-Ting Chung
Apr 16, 1998·Biochemical and Biophysical Research Communications·J W LinS F Weng
Dec 17, 1997·Biochemical and Biophysical Research Communications·S F WengY H Tseng
Jun 9, 2001·Biochemical and Biophysical Research Communications·J W LinS F Weng
Jan 27, 2004·Biochemical and Biophysical Research Communications·Shu-Fen WengJuey-Wen Lin
Aug 26, 2011·Molecular Phylogenetics and Evolution·Tory A Hendry, Paul V Dunlap

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