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首页> 外文期刊>Journal of bacteriology >Secretion of the Serratia marcescens HasA protein by an ABC transporter.
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Secretion of the Serratia marcescens HasA protein by an ABC transporter.

机译：ABC转运蛋白分泌粘质沙雷氏菌HasA蛋白。

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We previously identified a Serratia marcescens extracellular protein, HasA, able to bind heme and required for iron acquisition from heme and hemoglobin by the bacterium. This novel type of extracellular protein does not have a signal peptide and does not show sequence similarities to other proteins. HasA secretion was reconstituted in Escherichia coli, and we show here that like many proteins lacking a signal peptide, HasA has a C-terminal targeting sequence and is secreted by a specific ATP binding cassette (ABC) transporter consisting of three proteins, one inner membrane protein with a conserved ATP binding domain, called the ABC; a second inner membrane protein; and a third, outer membrane component. Since the three S. marcescens components of the HasA transporter have not yet been identified, the reconstituted HasA secretion system is a hybrid. It consists of the two S. marcescens inner membrane-specific components, HasD and HasE, associated with an outer membrane component coming from another bacterial ABC transporter, such as the E. coli TolC protein, the outer membrane component of the hemolysin transporter, or the Erwinia chrysanthemi PrtF protein, the outer membrane component of the protease transporter. This hybrid transporter was first shown to allow the secretion of the S. marcescens metalloprotease and the E. chrysanthemi metalloproteases B and C. On account of that, the two S. marcescens components HasD and HasE were previously named PrtDSM and PrtESM, respectively. However, HasA is secreted neither by the PrtD-PrtE-PrtF transporter (the genuine E. chrysanthemi protease transporter) nor by the HlyB-HlhD-TolC transporter (the hemolysin transporter). Moreover, HasA, coexpressed in the same cell, strongly inhibits the secretion of proteases B and C by their own transporter, indicating that the E. chrysanthemi transporter recognizes HasA. Since PrtF could replace TolC in the constitution of the HasA transporter, this indicates that the secretion block does not take place at the level of the outer membrane component but rather at an earlier step of interaction between HasA and the inner membrane components.
机译：我们以前鉴定了粘质沙雷氏菌的细胞外蛋白HasA，它能够结合血红素，并且是细菌从血红素和血红蛋白中获取铁所必需的。这种新型的细胞外蛋白没有信号肽，并且与其他蛋白没有序列相似性。 HasA分泌在大肠杆菌中重构，我们在这里表明，与许多缺乏信号肽的蛋白质一样，HasA具有C端靶向序列，并由由三种蛋白质（一个内膜）组成的特定ATP结合盒（ABC）转运蛋白分泌。具有保守的ATP结合域的蛋白质，称为ABC;第二内膜蛋白;第三，外膜组件。由于尚未鉴定出HasA转运蛋白的三个葡萄球菌成分，因此重组后的HasA分泌系统是杂种。它由两个marcescens内膜特定菌成分HasD和HasE组成，它们与来自另一个细菌ABC转运蛋白的外膜组分相关，例如大肠杆菌TolC蛋白，溶血素转运蛋白的外膜组分，或菊花欧文氏菌PrtF蛋白，蛋白酶转运蛋白的外膜成分。该杂合转运蛋白首先被证明可以分泌marcescens金属蛋白酶和chrysanthemi金属蛋白酶B和C。因此，marcescens的两个组分HasD和HasE先前分别命名为PrtDSM和PrtESM。但是，HasA既不被PrtD-PrtE-PrtF转运蛋白（真正的大肠杆菌蛋白酶转运蛋白）分泌，也不被HlyB-HlhD-TolC转运蛋白（溶血素转运蛋白）分泌。此外，在同一细胞中共表达的HasA通过其自身的转运蛋白强烈抑制蛋白酶B和C的分泌，表明金黄色葡萄球菌转运蛋白可识别HasA。由于PrtF可以替代HasA转运蛋白的成分中的TolC，因此表明分泌阻滞不是发生在外膜成分的水平，而是发生在HasA与内膜成分之间相互作用的较早步骤。

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