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

@article{citeulike:960978, abstract = {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.}, address = {Department of Microbiology, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, 9751 NN Haren, The Netherlands.}, author = {Albers, Sonja-Verena V. and Szab\'{o}, Zal\'{a}n and Driessen, Arnold J.}, citeulike-article-id = {960978}, citeulike-linkout-0 = {http://view.ncbi.nlm.nih.gov/pubmed/12813086}, citeulike-linkout-1 = {http://www.hubmed.org/display.cgi?uids=12813086}, issn = {0021-9193}, journal = {Journal of bacteriology}, keywords = {archaea, flagella, flagellin, pili, pilin, signal\_peptidase, signal\_peptide, sulfolobus, typeiv}, month = {July}, number = {13}, pages = {3918--3925}, posted-at = {2009-09-03 12:49:18}, priority = {2}, title = {Archaeal homolog of bacterial type IV prepilin signal peptidases with broad substrate specificity.}, url = {http://view.ncbi.nlm.nih.gov/pubmed/12813086}, volume = {185}, year = {2003} }

TY - JOUR ID - citeulike:960978 L3 - citeulike-article-id:960978 N2 - 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. IS - 13 JF - Journal of bacteriology SN - 0021-9193 AD - Department of Microbiology, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, 9751 NN Haren, The Netherlands. EP - 3925 TI - Archaeal homolog of bacterial type IV prepilin signal peptidases with broad substrate specificity. VL - 185 SP - 3918 KW - archaea KW - flagella KW - flagellin KW - pili KW - pilin KW - signal_peptidase KW - signal_peptide KW - sulfolobus KW - typeiv AU - Albers, Sonja-Verena AU - Szabó, Zalán AU - Driessen, Arnold PY - 2003/07// UR - http://view.ncbi.nlm.nih.gov/pubmed/12813086 ER -