Zobrazeno 1 - 10
of 40
pro vyhledávání: '"Mary C. Betlach"'
Autor:
Rainer Ziermann, Mary C. Betlach
Publikováno v:
BioTechniques, Vol 26, Iss 1, Pp 106-110 (1999)
Efficient polyketide synthesis derived from plasmid-borne heterologous Streptomyces polyketide synthase (PKS) gene clusters necessitates a suitable host strain. Wellcharacterized laboratory strains such as Streptomyces coelicolor or Streptomyces livi
Externí odkaz:
https://doaj.org/article/f2174c0c927a4a7a890c2a456ea2ff52
Publikováno v:
Biochemistry. 37:14937-14942
The post-polyketide synthase (PKS) biosynthetic tailoring of macrolide antibiotics usually involves one or more oxidation reactions catalyzed by cytochrome P450 monooxygenases. As the specificities of members from this class of enzymes vary significa
Publikováno v:
Molecular Microbiology. 16:357-364
Summary The bacterio-opsin gene (bop) of Halobacterium halobium is located within a cluster with three other genes. Growth conditions of high light intensity and low oxygen tension induce bop gene cluster expression. To identify putative regulatory f
Autor:
Felix Gropp, Mary C. Betlach
Publikováno v:
Proceedings of the National Academy of Sciences. 91:5475-5479
Oxygen and light affect the expression of the bacterioopsin gene (bop), which encodes a light-driven proton pump in the purple membrane of Halobacterium halobium. This response is thought to be mediated by a set of genes located adjacent to the bop g
Autor:
Richard F. Shand, Alok K. Mitra, Mary C. Betlach, Robert M. Stroud, George J. Turner, Larry J. W. Miercke
Publikováno v:
Scopus-Elsevier
Highly ordered two-dimensional (2-D) crystals of Escherichia coli-expressed bacteriorhodopsin analog (e-bR) and its D96N variant (e-D96N) reconstituted in Halobacterium halobium lipids have been obtained by starting with the opsin protein purified in
Publikováno v:
Systematic and Applied Microbiology. 16:716-724
Summary We have detected an additional gene in the bop gene cluster of the halophilic archaeon, Halobacterium halobium . This gene, denoted blp ( bacterio - o psin l inked p roduct) is located directly beyond the 3′ terminus of the bat gene and is
Autor:
Felix Gropp, Mary C. Betlach
Publikováno v:
Systematic and Applied Microbiology. 16:712-715
Summary The protein, bacterio-opsin, complexed with retinal functions as a light-driven proton pump in the purple membrane of the halophilic archaeon, Halobacterium halobium . The gene encoding bacterio-opsin ( bop ) is located within a cluster of ge
Autor:
Mary C. Betlach, Steven J. Milder, Thorgeir E. Thorgeirsson, Larry J. W. Miercke, Robert M. Stroud, Richard F. Shand, David S. Kliger
Publikováno v:
Biochemistry. 30:9133-9142
Bacteriorhodopsin (BR) with the single-site substitutions Arg-82----Gln (R82Q), Asp-85----Asn (D85N), and Asp-96----Asn (D96N) is studied with time-resolved absorption spectroscopy in the time regime from nanoseconds to seconds. Time-resolved spectra
Autor:
Mary C. Betlach, R F Shand
Publikováno v:
Journal of Bacteriology. 173:4692-4699
The bop gene cluster consists of at least three genes: bop (bacterio-opsin), brp (bacterio-opsin-related protein), and bat (bacterio-opsin activator). We have quantitated transcript levels from these genes in a wild-type and bacterioruberin-deficient
Autor:
Mary C. Betlach, Robert M. Stroud, Larry J. W. Miercke, Susan K. Fong, Richard F. Shand, Alok K. Mitra
Publikováno v:
Biochemistry. 30:3082-3088
The integral membrane protein bacterioopsin, found in the extremely halophilic archaebacterium Halobacterium halobium, was expressed in Escherichia coli as a fusion protein containing 13 heterologous amino acids at the amino terminus. The expressed p