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

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

Journal of bacteriology (2003-06-19)
Sonja-Verena Albers, Zalán Szabó, Arnold J M Driessen
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 PibD. 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.

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Roche
异丙基-β-d-半乳糖苷, mol wt 238.3, pkg of 1 g (10724815001), pkg of 5 g (11411446001)