| Gene structure and extracellular secretion of Neisseria gonorrhoeae IgA protease. | |
| | |
MedLine Citation:
|
PMID: 3027577 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
|
Several human bacterial pathogens, including the Gram-negative diplococcus Neisseria gonorrhoeae, produce extracellular proteases that are specific for human immunoglobulin IgA1. Immunoglobulin A (IgA) proteases have been studied extensively and the genes of some species cloned in Escherichia coli, but their role in pathogenesis remains unclear. Recently we derived a DNA fragment of 5 kilobases (kb) from N. gonorrhoeae MS11 directing extracellular active enzyme in E. coli. Although the mature enzyme of strain MS11 was shown to have a relative molecular mass of 106,000 (Mr 106K) in gels, the DNA sequence of this cloned fragment reveals a single gene coding for a 169K precursor of IgA protease. The precursor contains three functional domains, the amino-terminal leader which is assumed to initiate the inner membrane transport of the precursor, the protease, and a carboxyl-terminal 'helper' domain apparently required for extracellular secretion (excretion). Based on the structural features of the precursor, we propose a model in which the helper serves as a pore for excretion of the protease domain through the outer membrane. IgA protease acquires an active conformation as its extracellular transport proceeds and is released as a proform from the membrane-bound helper by autoproteolysis. The soluble proform further matures into the 106 K IgA protease and a small stable alpha-protein. |
| | |
Authors:
|
J Pohlner; R Halter; K Beyreuther; T F Meyer |
Related Documents
:
|
8403847 - Fibrinogenolytic proteases from the venoms of juvenile and adult northern pacific rattl... 16932887 - Characterization of proteolytic bacteria from the aleutian deep-sea and their proteases. 18824507 - Unconventional serine proteases: variations on the catalytic ser/his/asp triad configur... 7664477 - Ligand western blotting for specific detection of active forms of proteases. 12220197 - Localization of subunits d, e, and g in the yeast v-atpase complex using cysteine-media... 2753127 - Butylmalonate is a transition state analogue for aminocylase i. |
Publication Detail:
|
Type: Journal Article; Research Support, Non-U.S. Gov't |
Journal Detail:
|
Title: Nature Volume: 325 ISSN: 0028-0836 ISO Abbreviation: Nature Publication Date: 1987 Jan 29-Feb 4 |
Date Detail:
|
Created Date: 1987-03-12 Completed Date: 1987-03-12 Revised Date: 2006-11-15 |
Medline Journal Info:
|
Nlm Unique ID: 0410462 Medline TA: Nature Country: ENGLAND |
Other Details:
|
Languages: eng Pagination: 458-62 Citation Subset: IM |
| Data Bank Information | |
Bank Name/Acc. No.:
|
GENBANK/X04835 |
Export Citation:
|
APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
|
Amino Acid Sequence Base Sequence DNA Restriction Enzymes Escherichia coli / genetics Genes* Genes, Bacterial* Neisseria gonorrhoeae / enzymology*, genetics Peptide Hydrolases / genetics*, metabolism Protein Conformation Serine Endopeptidases* |
| Chemical | |
Reg. No./Substance:
|
EC 3.1.21.-/DNA Restriction Enzymes; EC 3.4.-/Peptide Hydrolases; EC 3.4.21.-/Serine Endopeptidases; EC 3.4.21.72/IgA-specific serine endopeptidase |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
Previous Document: Activation of sodium-proton exchange is a prerequisite for Ca2+ mobilization in human platelets.
Next Document: Transforming potential of the c-fms proto-oncogene (CSF-1 receptor).