| Archaeal homolog of bacterial type IV prepilin signal peptidases with broad substrate specificity. | |
| | |
MedLine Citation:
|
PMID: 12813086 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
|
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. |
| | |
Authors:
|
Sonja-Verena Albers; Zalán Szabó; Arnold J M Driessen |
Related Documents
:
|
3323846 - The escherichia coli cell division proteins ftsy, ftse and ftsx are inner membrane-asso... 3034606 - Import of frog prepropeptide gla into microsomes requires atp but does not involve dock... 10921896 - Elongation arrest is a physiologically important function of signal recognition particle. 16843006 - Alanine racemase from the acidophile acetobacter aceti. 6509936 - Purification and properties of pyruvate kinase from liver of the flounder (platichthys ... 12668726 - Bro1 is an endosome-associated protein that functions in the mvb pathway in saccharomyc... |
Publication Detail:
|
Type: Journal Article; Research Support, Non-U.S. Gov't |
Journal Detail:
|
Title: Journal of bacteriology Volume: 185 ISSN: 0021-9193 ISO Abbreviation: J. Bacteriol. Publication Date: 2003 Jul |
Date Detail:
|
Created Date: 2003-06-18 Completed Date: 2003-07-10 Revised Date: 2009-11-18 |
Medline Journal Info:
|
Nlm Unique ID: 2985120R Medline TA: J Bacteriol Country: United States |
Other Details:
|
Languages: eng Pagination: 3918-25 Citation Subset: IM |
Affiliation:
|
Department of Microbiology, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, 9751 NN Haren, The Netherlands. |
Export Citation:
|
APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
|
Amino Acid Sequence Archaeal Proteins / chemistry, genetics, metabolism* Bacterial Proteins / chemistry, genetics*, metabolism Endopeptidases / chemistry, genetics, metabolism* Escherichia coli / enzymology, genetics Membrane Proteins / chemistry, genetics, metabolism Molecular Sequence Data Mutagenesis, Site-Directed Protein Precursors / metabolism Protein Sorting Signals / genetics Sequence Alignment Sequence Homology, Amino Acid* Substrate Specificity Sulfolobus / enzymology*, genetics |
| Chemical | |
Reg. No./Substance:
|
0/Archaeal Proteins; 0/Bacterial Proteins; 0/Membrane Proteins; 0/Protein Precursors; 0/Protein Sorting Signals; EC 3.4.-/Endopeptidases; EC 3.4.99.-/type IV prepilin peptidase |
| Comments/Corrections | |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
Previous Document: Expression of spoIIIJ in the prespore is sufficient for activation of sigma G and for sporulation in...
Next Document: Transcriptional regulation of the gene encoding an alcohol dehydrogenase in the archaeon Sulfolobus ...