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פותח על ידי קלירמאש פתרונות בע"מ -
Cloning, expression, and purification of functional Sec11a and Sec11b, type I signal peptidases of the archaeon Haloferax volcanii
Year:
2006
Source of publication :
Journal of Bacteriology
Authors :
יריחימוביץ', ורד
;
.
Volume :
188
Co-Authors:
Fine, A., Department of Life Sciences, Ben Gurion University, Beersheva 84105, Israel
Irihimovitch, V., Department of Life Sciences, Ben Gurion University, Beersheva 84105, Israel
Dahan, I., Department of Life Sciences, Ben Gurion University, Beersheva 84105, Israel
Konrad, Z., Department of Life Sciences, Ben Gurion University, Beersheva 84105, Israel
Eichler, J., Department of Life Sciences, Ben Gurion University, Beersheva 84105, Israel, Dept. of Life Sciences, Ben Gurion University, P.O. Box 653, Beersheva 84105, Israel
Facilitators :
From page:
1911
To page:
1919
(
Total pages:
9
)
Abstract:
Across evolution, type I signal peptidases are responsible for the cleavage of secretory signal peptides from proteins following their translocation across membranes. In Archaea, type I signal peptidases combine domain-specific features with traits found in either their eukaryal or bacterial counterparts. Eukaryal and bacterial type I signal peptidases differ in terms of catalytic mechanism, pharmacological profile, and oligomeric status. In this study, genes encoding See11a and See11b, two type I signal peptidases of the halophilic archaeon Haloferax volcanii, were cloned. Although both genes are expressed in cells grown in rich medium, gene deletion approaches suggest that Sec11b, but not Sec11a, is essential. For purification purposes, tagged versions of the protein products of both genes were expressed in transformed Haloferax volcanii, with Sec11a and Sec11b being fused to a cellulose-binding domain capable of interaction with cellulose in hypersaline surroundings. By employing an in vitro signal peptidase assay designed for use with high salt concentrations such as those encountered by halophilic archaea such as Haloferax volcanii, the signal peptide-cleaving activities off both isolated membranes and purified Sec11a and Sec11b were addressed. The results show that the two enzymes differentially cleave the assay substrate, raising the possibility that the Sec11a and Sec11b serve distinct physiological functions. Copyright © 2006, American Society for Microbiology. All Rights Reserved.
Note:
Related Files :
archaebacterium
Evolution
gene expression
Molecular Sequence Data
protein transport
signal peptidase
unclassified drug
עוד תגיות
תוכן קשור
More details
DOI :
10.1128/JB.188.5.1911-1919.2006
Article number:
Affiliations:
Database:
סקופוס
Publication Type:
מאמר
;
.
Language:
אנגלית
Editors' remarks:
ID:
23960
Last updated date:
02/03/2022 17:27
Creation date:
17/04/2018 00:04
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Scientific Publication
Cloning, expression, and purification of functional Sec11a and Sec11b, type I signal peptidases of the archaeon Haloferax volcanii
188
Fine, A., Department of Life Sciences, Ben Gurion University, Beersheva 84105, Israel
Irihimovitch, V., Department of Life Sciences, Ben Gurion University, Beersheva 84105, Israel
Dahan, I., Department of Life Sciences, Ben Gurion University, Beersheva 84105, Israel
Konrad, Z., Department of Life Sciences, Ben Gurion University, Beersheva 84105, Israel
Eichler, J., Department of Life Sciences, Ben Gurion University, Beersheva 84105, Israel, Dept. of Life Sciences, Ben Gurion University, P.O. Box 653, Beersheva 84105, Israel
Cloning, expression, and purification of functional Sec11a and Sec11b, type I signal peptidases of the archaeon Haloferax volcanii
Across evolution, type I signal peptidases are responsible for the cleavage of secretory signal peptides from proteins following their translocation across membranes. In Archaea, type I signal peptidases combine domain-specific features with traits found in either their eukaryal or bacterial counterparts. Eukaryal and bacterial type I signal peptidases differ in terms of catalytic mechanism, pharmacological profile, and oligomeric status. In this study, genes encoding See11a and See11b, two type I signal peptidases of the halophilic archaeon Haloferax volcanii, were cloned. Although both genes are expressed in cells grown in rich medium, gene deletion approaches suggest that Sec11b, but not Sec11a, is essential. For purification purposes, tagged versions of the protein products of both genes were expressed in transformed Haloferax volcanii, with Sec11a and Sec11b being fused to a cellulose-binding domain capable of interaction with cellulose in hypersaline surroundings. By employing an in vitro signal peptidase assay designed for use with high salt concentrations such as those encountered by halophilic archaea such as Haloferax volcanii, the signal peptide-cleaving activities off both isolated membranes and purified Sec11a and Sec11b were addressed. The results show that the two enzymes differentially cleave the assay substrate, raising the possibility that the Sec11a and Sec11b serve distinct physiological functions. Copyright © 2006, American Society for Microbiology. All Rights Reserved.
Scientific Publication
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