大肠杆菌酰基载体蛋白合成与翻译后修饰之间明显的偶联是由于氨基酸生物合成受到抑制。
The apparent coupling between synthesis and posttranslational modification of Escherichia coli acyl carrier protein is due to inhibition of amino acid biosynthesis.
作者信息
Keating D H, Zhang Y, Cronan J E
机构信息
Department of Microbiology, University of Illinois, Urbana 61801, USA.
出版信息
J Bacteriol. 1996 May;178(9):2662-7. doi: 10.1128/jb.178.9.2662-2667.1996.
Abstract
Acyl carrier protein (ACP) is modified on serine 36 by the covalent posttranslational attachment of 4'-phosphopantetheine from coenzyme A (CoA), and this modification is required for lipid biosynthesis. Jackowski and Rock (J. Biol. Chem 258:15186-15191, 1983) reported that upon depletion of the CoA pool by starvation for a CoA precursor, no accumulation of the unmodified form of ACP (apo-ACP) was detected. We report that this lack of apo-ACP accumulation results from decreased translation of the acpP mRNAs because of the limitation of the synthesis of glutamate and other amino acids made directly from tricarboxylic acid cycle intermediates.
摘要
酰基载体蛋白（ACP）在丝氨酸36处通过来自辅酶A（CoA）的4'-磷酸泛酰巯基乙胺的共价翻译后连接进行修饰，这种修饰是脂质生物合成所必需的。杰科夫斯基和罗克（《生物化学杂志》258:15186 - 15191，1983年）报道，在用CoA前体饥饿使CoA库耗尽时，未检测到未修饰形式的ACP（脱辅基ACP）的积累。我们报道，脱辅基ACP积累的缺乏是由于acpP mRNA的翻译减少，这是因为谷氨酸和其他直接由三羧酸循环中间体合成的氨基酸的合成受到限制。
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