Archaeal homolog of bacterial type IV prepilin signal peptidases with broad substrate specificity

被引:109
作者
Albers, SV [1 ]
Szabó, Z [1 ]
Driessen, AJM [1 ]
机构
[1] Univ Groningen, Groningen Biomol Sci & Biotechnol Inst, Dept Microbiol, NL-9751 NN Haren, Netherlands
关键词
D O I
10.1128/JB.185.13.3918-3925.2003
中图分类号
Q93 [微生物学];
学科分类号
071005 ; 100705 ;
摘要
A large number of secretory proteins in the thermoacidophile Sulfolobus solfataricus are synthesized as a precursor with an unusual leader peptide that resembles bacterial type IV prepilin signal sequences. This set of proteins includes the flagellin subunit but also various solute binding proteins. Here we describe the identification of the S. solfataricus homolog of bacterial type IV prepilin peptidases, termed MD. PibD is an integral membrane protein that is phylogenetically related to the bacterial enzymes. When heterologously expressed in Escherichia coli, PibD is capable of processing both the flagellin and glucose-binding protein (GlcS) precursors. Site-directed mutagenesis of the GlcS signal peptide shows that the substrate specificity of PibD is consistent with the variations found in proteins with type IV prepilin-like signal sequences of S. solfataricus. We conclude that PibD is responsible for the processing of these secretory proteins in S. solfataricus.
引用
收藏
页码:3918 / 3925
页数:8
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