Structural and functional analysis of Bacillus subtilis YisP reveals a role of its product in biofilm production.

Structural and functional analysis of Bacillus subtilis YisP reveals a role of its product in biofilm production.
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DOI:
10.1016/j.chembiol.2014.08.018
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发表时间:
2014-11-20
影响因子:
--
通讯作者:
Oldfield E
Oldfield E
中科院分区:
生物1区
文献类型:
--
作者:
Feng X;Hu Y;Zheng Y;Zhu W;Li K;Huang CH;Ko TP;Ren F;Chan HC;Nega M;Bogue S;López D;Kolter R;Götz F;Guo RT;Oldfield E

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YisP参与枯草芽孢杆菌中的生物膜形成,并且已经预测产生C30类异戊二烯。我们确定了YisP的结构,并观察到它采用与角鲨烯和脱氢角鲨烯脱氢酶相同的折叠。然而,在基本上所有类异戊二烯脱氢酶中发现的第一个富酒石酸基序在YisP中是贫酒石酸基序,并且不能催化头对头缩合反应。我们发现,YisP作为一种磷酸酶,催化形成法呢醇从法呢基二磷酸,是第一个磷酸酶采取的折叠头到头异戊二烯基脱氢酶。法尼醇在Δyisp突变体中恢复生物膜形成,并类似于毒力因子葡萄球菌黄素改变脂质膜结构。这项工作阐明了YisP在生物膜形成中的作用,并提出了一种有趣的可能性,即在其他细菌中发现的许多YisP样同系物也可能具有有趣的产物和功能。
YisP is involved in biofilm formation in Bacillus subtilis and has been predicted to produce C30 isoprenoids. We determined the structure of YisP and observe that it adopts the same fold as squalene and dehydrosqualene synthases. However, the first aspartate-rich motif found in essentially all isoprenoid synthases is aspartate-poor in YisP, and cannot catalyze head-to-head condensation reactions. We find that YisP acts as a phosphatase, catalyzing formation of farnesol from farnesyl diphosphate, and is the first phosphatase to adopt the fold seen in the head-to-head prenyl synthases. Farnesol restores biofilm formation in a Δyisp mutant, and modifies lipid membrane structure similarly to the virulence factor, staphyloxanthin. The work clarifies the role of YisP in biofilm formation and suggests an intriguing possibility that many of the YisP-like homologs found in other bacteria may also have interesting products and functions.
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