scholarly journals Cloning and sequencing of a gene encoding a glutamate and aspartate carrier of Escherichia coli K-12.

1990 ◽  
Vol 172 (6) ◽  
pp. 3214-3220 ◽  
Author(s):  
B Wallace ◽  
Y J Yang ◽  
J S Hong ◽  
D Lum
Gene ◽  
1993 ◽  
Vol 133 (1) ◽  
pp. 109-113 ◽  
Author(s):  
Nishimura Koichi ◽  
Nakayashiki Toru ◽  
Inokuchi Hachiro

1986 ◽  
Vol 261 (32) ◽  
pp. 14929-14935
Author(s):  
J W Chase ◽  
B A Rabin ◽  
J B Murphy ◽  
K L Stone ◽  
K R Williams

Microbiology ◽  
2020 ◽  
Vol 166 (9) ◽  
pp. 880-890 ◽  
Author(s):  
Hiroshi Ogasawara ◽  
Toshiyuki Ishizuka ◽  
Shuhei Hotta ◽  
Michiko Aoki ◽  
Tomohiro Shimada ◽  
...  

Under stressful conditions, Escherichia coli forms biofilm for survival by sensing a variety of environmental conditions. CsgD, the master regulator of biofilm formation, controls cell aggregation by directly regulating the synthesis of Curli fimbriae. In agreement of its regulatory role, as many as 14 transcription factors (TFs) have so far been identified to participate in regulation of the csgD promoter, each monitoring a specific environmental condition or factor. In order to identify the whole set of TFs involved in this typical multi-factor promoter, we performed in this study ‘promoter-specific transcription-factor’ (PS-TF) screening in vitro using a set of 198 purified TFs (145 TFs with known functions and 53 hitherto uncharacterized TFs). A total of 48 TFs with strong binding to the csgD promoter probe were identified, including 35 known TFs and 13 uncharacterized TFs, referred to as Y-TFs. As an attempt to search for novel regulators, in this study we first analysed a total of seven Y-TFs, including YbiH, YdcI, YhjC, YiaJ, YiaU, YjgJ and YjiR. After analysis of curli fimbriae formation, LacZ-reporter assay, Northern-blot analysis and biofilm formation assay, we identified at least two novel regulators, repressor YiaJ (renamed PlaR) and activator YhjC (renamed RcdB), of the csgD promoter.


Gene ◽  
1995 ◽  
Vol 160 (1) ◽  
pp. 101-103 ◽  
Author(s):  
Carol E. Jones ◽  
Toni M. Fleming ◽  
Peter W. Piper ◽  
Jennifer A. Littlechild ◽  
Don A. Cowan

1988 ◽  
Vol 170 (12) ◽  
pp. 5901-5907 ◽  
Author(s):  
R Lahti ◽  
T Pitkäranta ◽  
E Valve ◽  
I Ilta ◽  
E Kukko-Kalske ◽  
...  

2006 ◽  
Vol 188 (17) ◽  
pp. 6435-6439 ◽  
Author(s):  
Melissa Gulmezian ◽  
Haitao Zhang ◽  
George T. Javor ◽  
Catherine F. Clarke

ABSTRACT IS16 is a thiol-sensitive, Q-deficient mutant strain of Escherichia coli. Here, we show that IS16 harbors a mutation in the ubiG gene encoding a methyltransferase required for two O-methylation steps of Q biosynthesis. Complementation of IS16 with either ubiG or ubiX K-12 reverses this phenotype, suggesting that UbiX may interact with UbiG.


1989 ◽  
Vol 264 (2) ◽  
pp. 397-402 ◽  
Author(s):  
A F Alwan ◽  
B I A Mgbeje ◽  
P M Jordan

The Escherichia coli hemD gene, encoding the enzyme uroporphyrinogen III synthase (co-synthase), was cloned into multi-copy plasmids in E. coli cells that were used to generate strains producing up to 1000 times the concentration of the synthase in the wild-type. The enzyme was purified to homogeneity from these strains in milligram amounts. The enzyme is a monomer of Mr 28,000 with an isoelectric point of 5.2 and a pH optimum of 7.8. The specific activity of the purified synthase is 1500 units/mg and the Km for the substrate, pre-uroporphyrinogen, is 5 microM. The N-terminal sequence of the enzyme is Ser-Ile-Leu-Val-Thr-Arg-Pro-Ser-Pro-Ala-Gly-, in agreement with the gene-derived protein sequence. The enzyme contains four 5,5′-dithiobis-(2-nitrobenzoic acid)-titratable groups, one reacting rapidly with the reagent and three further groups having lower reactivity. The enzyme is heat-sensitive, and during heat inactivation all four thiol groups become equally available for reaction.


Genetics ◽  
1996 ◽  
Vol 143 (2) ◽  
pp. 627-635 ◽  
Author(s):  
Maryann Giel ◽  
Martine Desnoyer ◽  
Jane Lopilato

Abstract A new mutation, bglJ4, has been characterized that results in the expression of the silent bgl operon. The bgl operon encodes proteins necessary for the transport and utilization of the aromatic β-glucosides arbutin and salicin. A variety of mutations activate the operon and result in a Bgl+ phenotype. Activating mutations are located upstream of the bgl promoter and in genes located elsewhere on the chromosome. Mutations outside of the bgl operon occur in the genes encoding DNA gyrase and in the gene encoding the nucleoid associated protein H-NS. The mutation described here, bglJ4, has been mapped to a new locus at min 99 on the Escherichia coli K-12 genetic map. The putative protein encoded by the bgygene has homolgy to a family of transcriptional activators. Evidence is presented that increased expression of the bglJ product is needed for activation of the bgl operon.


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