The Experts below are selected from a list of 1722 Experts worldwide ranked by ideXlab platform
A Janulaitis - One of the best experts on this subject based on the ideXlab platform.
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BfiI, a restriction endonuclease from Bacillus Firmus S8120, which recognizes the novel non-palindromic sequence 5′-ACTGGG(N)5/4-3′
Nucleic acids research, 1998Co-Authors: J Vitkute, Z Maneliene, M Petrusyte, A JanulaitisAbstract:A new type IIS restriction endonuclease Bfi I hasbeen partially purified from Bacillus Firmus S8120. Bfi I recognizes the non-palindromic hexanucleotide sequence 5'-ACTGGG(N)5/4-3' and makes a staggered cut at the fifth base pair downstream of the recognition sequence on the upper strand, producing a single base 3' protruding end.
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bfii a restriction endonuclease from Bacillus Firmus s8120 which recognizes the novel non palindromic sequence 5 actggg n 5 4 3
Nucleic Acids Research, 1998Co-Authors: J Vitkute, Z Maneliene, M Petrusyte, A JanulaitisAbstract:A new type IIS restriction endonuclease Bfi I hasbeen partially purified from Bacillus Firmus S8120. Bfi I recognizes the non-palindromic hexanucleotide sequence 5'-ACTGGG(N)5/4-3' and makes a staggered cut at the fifth base pair downstream of the recognition sequence on the upper strand, producing a single base 3' protruding end.
J Vitkute - One of the best experts on this subject based on the ideXlab platform.
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BfiI, a restriction endonuclease from Bacillus Firmus S8120, which recognizes the novel non-palindromic sequence 5′-ACTGGG(N)5/4-3′
Nucleic acids research, 1998Co-Authors: J Vitkute, Z Maneliene, M Petrusyte, A JanulaitisAbstract:A new type IIS restriction endonuclease Bfi I hasbeen partially purified from Bacillus Firmus S8120. Bfi I recognizes the non-palindromic hexanucleotide sequence 5'-ACTGGG(N)5/4-3' and makes a staggered cut at the fifth base pair downstream of the recognition sequence on the upper strand, producing a single base 3' protruding end.
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bfii a restriction endonuclease from Bacillus Firmus s8120 which recognizes the novel non palindromic sequence 5 actggg n 5 4 3
Nucleic Acids Research, 1998Co-Authors: J Vitkute, Z Maneliene, M Petrusyte, A JanulaitisAbstract:A new type IIS restriction endonuclease Bfi I hasbeen partially purified from Bacillus Firmus S8120. Bfi I recognizes the non-palindromic hexanucleotide sequence 5'-ACTGGG(N)5/4-3' and makes a staggered cut at the fifth base pair downstream of the recognition sequence on the upper strand, producing a single base 3' protruding end.
Terry A. Krulwich - One of the best experts on this subject based on the ideXlab platform.
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Reidentification of facultatively alkaliphilic Bacillus Firmus OF4 as Bacillus pseudoFirmus OF4.
Extremophiles : life under extreme conditions, 2000Co-Authors: Hideto Takami, Terry A. KrulwichAbstract:With a view toward verifying the original classification of alkaliphilic Bacillus Firmus OF4, physiological and biochemical characteristics were more extensively catalogued than in original studies, and this catalog was supplemented with 16S rDNA sequence homology and more extensive DNA–DNA hybridization analyses. Phylogenetic analysis of this alkaliphile based on the comparison of multiple 16S rDNA sequences from Bacillus species indicated that this strain is most closely related to Bacillus pseudoFirmus. Consistently, in the DNA–DNA hybridization analysis of the alkaliphile and Bacillus reference strains, the highest level of DNA–DNA relatedness (96%) was found between the alkaliphile and the B. pseudoFirmus type strain (DSM 8715T). The findings support the conclusion that this alkaliphile strain is more closely related to B. pseudoFirmus than to B. Firmus, and we propose the future use of the designation B. pseudoFirmus OF4.
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Physical map of alkaliphilic Bacillus Firmus OF4 and detection of a large endogenous plasmid
Extremophiles : life under extreme conditions, 1998Co-Authors: Anne Grønstad, Terry A. Krulwich, Michael G. Sturr, Masahiro Ito, Ewa Jaroszewicz, Anne-brit KolstøAbstract:Extremely alkaliphilic Bacillus Firmus OF4 is among the best characterized of this group of alkaliphiles. Together with alkaliphilic Bacillus C-125 and numerous non-alkaliphilic Bacillus species whose chromosomes and gene organizations are currently being studied in detail, work on B. Firmus OF4 offers the opportunity to discern whether there are features of chromosome and gene organization that are associated with alkaliphily. A physical map of the B. Firmus OF4 is consistent with a circular chromosome of approximately 4 Mb, with an extrachromosomal element of 110 kb also detected. The previously identified cadmium-resistance locus and transposition functions in B. Firmus OF4 were localized to the extrachromosomal element, whose genes exhibit a slightly different pattern of codon usage from chromosomal genes. No clustering of genes thus far identified with roles in alkaliphily has been found. Direct repeat sequences (DRS) were previously reported upstream of a gene encoding a Na+/H+ antiporter that has a role in pH homeostasis. In the current analyses, these sequences were found to be present in multiple copies on the chromosome, most of which are present in one 920-kb fragment. Such sequences might play a role in DNA rearrangements that allow amplification of important genes in this region.
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Diverse genes of alkaliphilic Bacillus Firmus OF4 that complement K+-uptake-deficient Escherichia coli include an ftsH homologue
Extremophiles : life under extreme conditions, 1997Co-Authors: Masahiro Ito, Benjamin Cooperberg, Terry A. KrulwichAbstract:Seven clones isolated from libraries of DNA from alkaliphilic Bacillus Firmus OF4 restored the growth of a K+-uptake-deficient Escherichia coli mutant on only 10mM K+. None of the clones contained genes with apparent homology to known K+ transport systems in other organisms. Based on sequence homologies, the newly isolated alkaliphile loci included: ftsH; a dipeptide transport system; a gerC locus with hydrophobic open reading frames not found in the comparable locus of Bacillus subtilis; a sugar phosphotransferase enzyme; and a capBC homologue. The ftsH gene provided a new and striking example of a recognized property of extracellular and external regions of polytopic alkaliphile proteins: a significant paucity of basic amino acid residues relative to neutrophile counterparts. The alkaliphile ftsH gene was able to complement a mutant of E. coli with a temperature-sensitive ftsH gene product.
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Purification and characterization of the succinate dehydrogenase complex and CO-reactive b-type cytochromes from the facultative alkaliphile Bacillus Firmus OF4
Biochimica et biophysica acta, 1996Co-Authors: Raymond Gilmour, Terry A. KrulwichAbstract:The presence of a bo-type terminal oxidase in Bacillus Firmus OF4 had been suggested from the effects of CO on the spectra of reduced membrane cytochromes (Hicks, D.B., Plass, R.J. and Quirk, P.G. (1991) J. Bacteriol. 173, 5010–5016). In that study the CO-binding b-type cytochrome was partially purified by anion exchange chromatography. No further purification was attempted but later HPLC analysis indicated the absence of significant heme O in the B. Firmus OF4 membranes. The current work shows that the partially purified cytochrome b is actually composed of three different b-type cytochromes which can be separated and purified by a combination of ion-exchange, hydroxyapatite and gel filtration chromatographies. Two of the cytochromes were CO-reactive but lacked the characteristic multisubunit composition of known terminal oxidases. Neither purified cytochrome catalyzed quinol or ferrocytochrome c oxidation. The more abundant CO-reactive b-type cytochrome (cytochrome b560) had an apparent molecular mass of 10 kDa, whereas the other, more minor component (cytochrome b558), was partially purified and showed two bands of 23 and 17 kDa on SDS-PAGE. The functions of the cytochromes b560 and b558 remain unknown but together they account for the spectrum originally attributed to cytochrome bo. The third, non-CO reactive, cytochrome b, was associated with substantial succinate dehydrogenase activity and was purified as a three subunit succinate dehydrogenase complex with high specific activity (17.7 μmol/min/mg). Limited N-terminal sequence of each subunit demonstrated marked similarity to the complex from Bacillus subtilis. The cytochrome b of the alkaliphile enzyme was reduced about 50% by succinate compared to the level of reduction achieved by dithionite. The enzyme reacted with both napthoquinones and benzoquinones. The results presented indicate that Bacillus Firmus OF4 contains a succinate dehydrogenase complex with very similar properties to the enzyme from Bacillus subtilis, but does not contain a cytochrome o-type terminal oxidase under the growth conditions studied.
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Oxidative phosphorylation by ADP + P(i)-loaded membrane vesicles of alkaliphilic Bacillus Firmus OF4.
The Journal of biological chemistry, 1994Co-Authors: Arthur A. Guffanti, Terry A. KrulwichAbstract:ATP synthesis in ADP + P(i)-loaded membrane vesicles of the facultative alkaliphile Bacillus Firmus OF4 at an external pH of 10.5 did not depend upon the presence of cell wall polymers, e.g. as a proton barrier or sequestration device. Upon energization with ascorbate plus phenazine methosulfate, vesicles at pH(out) = 7.5 generated an electrochemical proton gradient (delta p) of -160 mV, acid and positive out, whereas at pH(out) = 10.5, the delta p was -40 mV, alkaline and positive out. Nonetheless, ATP synthesis was more rapid at the more alkaline pH value, especially in the presence of 200 mM K2SO4, which markedly lowered the surface potential. No synthesis was observed upon abolition of the delta p. Respiration-derived transmembrane potentials (delta psi) energized ATP synthesis much better than an equally large diffusion potential. The diffusion potential failed to energize ATP synthesis above pH 9.5. When delta p, all in the form of a delta psi, was titrated downward at either pH 7.8 or 9.5, ATP synthesis by the latter vesicles was much less adversely affected in the delta p range of -150 to -50 mV, supporting the existence of a sparing, non-chemiosmotic energy component at high pH.
Z Maneliene - One of the best experts on this subject based on the ideXlab platform.
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BfiI, a restriction endonuclease from Bacillus Firmus S8120, which recognizes the novel non-palindromic sequence 5′-ACTGGG(N)5/4-3′
Nucleic acids research, 1998Co-Authors: J Vitkute, Z Maneliene, M Petrusyte, A JanulaitisAbstract:A new type IIS restriction endonuclease Bfi I hasbeen partially purified from Bacillus Firmus S8120. Bfi I recognizes the non-palindromic hexanucleotide sequence 5'-ACTGGG(N)5/4-3' and makes a staggered cut at the fifth base pair downstream of the recognition sequence on the upper strand, producing a single base 3' protruding end.
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bfii a restriction endonuclease from Bacillus Firmus s8120 which recognizes the novel non palindromic sequence 5 actggg n 5 4 3
Nucleic Acids Research, 1998Co-Authors: J Vitkute, Z Maneliene, M Petrusyte, A JanulaitisAbstract:A new type IIS restriction endonuclease Bfi I hasbeen partially purified from Bacillus Firmus S8120. Bfi I recognizes the non-palindromic hexanucleotide sequence 5'-ACTGGG(N)5/4-3' and makes a staggered cut at the fifth base pair downstream of the recognition sequence on the upper strand, producing a single base 3' protruding end.
M Petrusyte - One of the best experts on this subject based on the ideXlab platform.
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BfiI, a restriction endonuclease from Bacillus Firmus S8120, which recognizes the novel non-palindromic sequence 5′-ACTGGG(N)5/4-3′
Nucleic acids research, 1998Co-Authors: J Vitkute, Z Maneliene, M Petrusyte, A JanulaitisAbstract:A new type IIS restriction endonuclease Bfi I hasbeen partially purified from Bacillus Firmus S8120. Bfi I recognizes the non-palindromic hexanucleotide sequence 5'-ACTGGG(N)5/4-3' and makes a staggered cut at the fifth base pair downstream of the recognition sequence on the upper strand, producing a single base 3' protruding end.
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bfii a restriction endonuclease from Bacillus Firmus s8120 which recognizes the novel non palindromic sequence 5 actggg n 5 4 3
Nucleic Acids Research, 1998Co-Authors: J Vitkute, Z Maneliene, M Petrusyte, A JanulaitisAbstract:A new type IIS restriction endonuclease Bfi I hasbeen partially purified from Bacillus Firmus S8120. Bfi I recognizes the non-palindromic hexanucleotide sequence 5'-ACTGGG(N)5/4-3' and makes a staggered cut at the fifth base pair downstream of the recognition sequence on the upper strand, producing a single base 3' protruding end.
