scholarly journals Laboratory evolution of Geobacter sulfurreducens for enhanced growth on lactate via a single-base-pair substitution in a transcriptional regulator

2011 ◽  
Vol 6 (5) ◽  
pp. 975-983 ◽  
Author(s):  
Zarath M Summers ◽  
Toshiyuki Ueki ◽  
Wael Ismail ◽  
Shelley A Haveman ◽  
Derek R Lovley
Keyword(s):  
Base Pair ◽  
Transcriptional Regulator ◽  
Geobacter Sulfurreducens ◽  
Laboratory Evolution ◽  
Single Base ◽  
Single Base Pair Substitution ◽  
Single Base Pair ◽  
Base Pair Substitution

A single-base-pair substitution abolishes d-amino-acid oxidase activity in the mouse

1992 ◽  
Vol 1139 (4) ◽  
pp. 315-318 ◽  
Author(s):  
Masato Sasaki ◽  
Ryuichi Konno ◽  
Masahiro Nihio ◽  
Akira Niwa ◽  
Yosihiro Yasumura ◽  
...  
Keyword(s):  
Amino Acid ◽  
Base Pair ◽  
Oxidase Activity ◽  
Acid Oxidase ◽  
Amino Acid Oxidase ◽  
Single Base ◽  
Single Base Pair Substitution ◽  
Single Base Pair ◽  
Base Pair Substitution

scholarly journals Systematic single base-pair substitution analysis of DNA binding by the cAMP receptor protein in cyanobacteriumSynechocystissp. PCC 6803

FEBS Letters ◽  
2004 ◽  
Vol 563 (1-3) ◽  
pp. 55-58 ◽  
Author(s):  
Katsumi Omagari ◽  
Hidehisa Yoshimura ◽  
Mitsunori Takano ◽  
Dongyun Hao ◽  
Masayuki Ohmori ◽  
...  
Keyword(s):  
Dna Binding ◽  
Base Pair ◽  
Receptor Protein ◽  
Camp Receptor Protein ◽  
Single Base ◽  
Single Base Pair Substitution ◽  
Single Base Pair ◽  
Base Pair Substitution ◽  
Camp Receptor ◽  
Pcc 6803

A single base pair substitution within the paired box of PAX3 in an individual with Waardenburg syndrome type 1 (WS1)

1994 ◽  
Vol 4 (3) ◽  
pp. 227-228 ◽  
Author(s):  
John W. Pierpont ◽  
Luke D. Doolan ◽  
Kurt Amann ◽  
Greg R. Snead ◽  
Robert P. Erickson
Keyword(s):  
Base Pair ◽  
Syndrome Type ◽  
Waardenburg Syndrome ◽  
Single Base ◽  
Single Base Pair Substitution ◽  
Single Base Pair ◽  
Base Pair Substitution

scholarly journals The Genes rubA and rubB for Alkane Degradation in Acinetobacter sp. Strain ADP1 Are in an Operon with estB, Encoding an Esterase, andoxyR

1999 ◽  
Vol 181 (14) ◽  
pp. 4292-4298 ◽  
Author(s):  
Walter Geißdörfer ◽  
Ruben G. Kok ◽  
Andreas Ratajczak ◽  
Klaas J. Hellingwerf ◽  
Wolfgang Hillen
Keyword(s):  
Hydrogen Peroxide ◽  
Base Pair ◽  
Transcriptional Regulator ◽  
Alkane Hydroxylase ◽  
Alkane Degradation ◽  
Single Base ◽  
Internal Promoter ◽  
Single Base Pair ◽  
Alkane Monooxygenase ◽  
Acinetobacter Sp

ABSTRACT Alkanes are oxidized in Acinetobacter sp. strain ADP1 by a three-component alkane monooxygenase, composed of alkane hydroxylase, rubredoxin, and rubredoxin reductase. rubA andrubB encode rubredoxin and a NAD(P)H-dependent rubredoxin reductase. We demonstrate here that single base pair substitutions inrubA or rubB lead to defects in alkane degradation, showing that both genes are essential for alkane utilization. Differences in the degradation capacity for hexadecane and dodecane in these mutants are discussed. Two genes, estBand oxyR, are located downstream of rubB, but are not necessary for alkane degradation. estB encodes a functional esterase. oxyR encodes a LysR-type transcriptional regulator, conferring resistance to hydrogen peroxide.rubA, rubB, estB, andoxyR constitute an operon, which is constitutively transcribed from a ς70 promoter, and anestB-oxyR containing message is also transcribed from an internal promoter.

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