標題: The ATP-binding motif in AcoK is required for regulation of acetoin catabolism in Klebsiella pneumoniae CG43
作者: Hsu, Jye-Lin
Peng, Hwei-Ling
Chang, Hwan-You
生物科技學系
Department of Biological Science and Technology
關鍵字: AcoK;acetoin dehydrogenase;STAND NTPase;ATP-binding motif;MalT
公開日期: 7-十一月-2008
摘要: Many bacterial species utilize acetoin as a carbon source. In Klebsiella pneumoniae, the utilization of acetoin is catalyzed by an acetoin dehydrogenase complex encoded by the acoABCD operon, which is positively regulated in the presence of acetoin by the transcriptional factor AcoK. AcoK contains a LuxR type DNA-binding domain at the C-terminal region and putative Walker A and B nucleotide-binding motifs in the N-terminal region. The comprehensive deletion and mutation study performed here shows that mutations in the putative Walker A motif result in a significant reduction of ATP hydrolysis and trans-activation by AcoK of acoABCD expression, presumably due to a loss of ATP-binding ability. AcoK was shown to bind specifically to nucleotides -66 to -36 of the acoABCD promoter, though the DNA-binding ability was not affected by the Walker A motif mutation. Thus, this study provides an additional example of how a member of the signal transduction ATPases with numerous domains family activates its target gene expression. (C) 2008 Elsevier Inc. All rights reserved.
URI: http://dx.doi.org/10.1016/j.bbrc.2008.08.103
http://hdl.handle.net/11536/8155
ISSN: 0006-291X
DOI: 10.1016/j.bbrc.2008.08.103
期刊: BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
Volume: 376
Issue: 1
起始頁: 121
結束頁: 127
顯示於類別:期刊論文


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