Literature DB >> 8383625

Homologous bacterio-opsin-encoding gene expression via site-specific vector integration.

E Ferrando1, U Schweiger, D Oesterhelt.   

Abstract

Homologous recombination in the archaebacterium Halobacterium halobium has been investigated and exploited for the wild-type (wt) level of expression of the bacterio-opsin-encoding gene (bop). The Haloferax volcanii-Escherichia coli shuttle vector, pWL102, was used to construct a shuttle-mutagenesis vector, pEF191, bearing bop and short flanking sequences. Transformation of a bacteriorhodopsin (BR)-negative H. halobium strain with pEF191 resulted in plasmid integration at the homologous bop locus. A model for this site-specific vector integration is presented which has been confirmed by determining the arrangement of the repeated homologous sequences on the chromosome. Two different configurations are obtained after integrative transformation due to the presence of an insertion element in the genomic copy of bop. In one configuration, the functional bop cluster containing the regulatory bat and brp genes was in wt arrangement. In the second configuration, the bop cluster is interrupted by 10 kb of plasmid vector sequences, and the upstream region required for bop expression was limited to 400 bp. The BR production for both configurations was determined and found to be at wt level. These results suggest that the function of the putative bop promoter does not depend on the defined upstream positions of bat and brp. The system presented here can be easily exploited for structure-function studies on BR and introduces homologous gene targeting as a powerful tool in the study of halobacterial genetics.

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Year:  1993        PMID: 8383625     DOI: 10.1016/0378-1119(93)90743-m

Source DB:  PubMed          Journal:  Gene        ISSN: 0378-1119            Impact factor:   3.688


  16 in total

1.  Time-resolved detection of transient movement of helices F and G in doubly spin-labeled bacteriorhodopsin.

Authors:  N Radzwill; K Gerwert; H J Steinhoff
Journal:  Biophys J       Date:  2001-06       Impact factor: 4.033

2.  Proton binding within a membrane protein by a protonated water cluster.

Authors:  Florian Garczarek; Leonid S Brown; Janos K Lanyi; Klaus Gerwert
Journal:  Proc Natl Acad Sci U S A       Date:  2005-02-28       Impact factor: 11.205

3.  Roles of cytoplasmic arginine and threonine in chloride transport by the bacteriorhodopsin mutant D85T.

Authors:  S Paula; J Tittor; D Oesterhelt
Journal:  Biophys J       Date:  2001-05       Impact factor: 4.033

4.  Proton transfer via a transient linear water-molecule chain in a membrane protein.

Authors:  Erik Freier; Steffen Wolf; Klaus Gerwert
Journal:  Proc Natl Acad Sci U S A       Date:  2011-06-27       Impact factor: 11.205

5.  Spin-labeling studies of the conformational changes in the vicinity of D36, D38, T46, and E161 of bacteriorhodopsin during the photocycle.

Authors:  T Rink; J Riesle; D Oesterhelt; K Gerwert; H J Steinhoff
Journal:  Biophys J       Date:  1997-08       Impact factor: 4.033

6.  Inversion of proton translocation in bacteriorhodopsin mutants D85N, D85T, and D85,96N.

Authors:  J Tittor; U Schweiger; D Oesterhelt; E Bamberg
Journal:  Biophys J       Date:  1994-10       Impact factor: 4.033

7.  Photoactive mitochondria: in vivo transfer of a light-driven proton pump into the inner mitochondrial membrane of Schizosaccharomyces pombe.

Authors:  A Hoffmann; V Hildebrandt; J Heberle; G Büldt
Journal:  Proc Natl Acad Sci U S A       Date:  1994-09-27       Impact factor: 11.205

8.  Molecular mechanism of protein-retinal coupling in bacteriorhodopsin.

Authors:  J K Delaney; U Schweiger; S Subramaniam
Journal:  Proc Natl Acad Sci U S A       Date:  1995-11-21       Impact factor: 11.205

9.  The bat gene of Halobacterium halobium encodes a trans-acting oxygen inducibility factor.

Authors:  F Gropp; M C Betlach
Journal:  Proc Natl Acad Sci U S A       Date:  1994-06-07       Impact factor: 11.205

10.  The archaebacterial membrane protein bacterio-opsin is expressed and N-terminally processed in the yeast Saccharomyces cerevisiae.

Authors:  C Lang-Hinrichs; I Queck; G Büldt; U Stahl; V Hildebrandt
Journal:  Mol Gen Genet       Date:  1994-07-25
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