Cloning and sequencing of a gene from the archaeon Pyrococcus furiosus with high homology to a gene encoding phosphoenolpyruvate synthetase from Escherichia coli

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
Keyword(s):  
Escherichia Coli ◽  
Pyrococcus Furiosus ◽  
High Homology ◽  
Cloning And Sequencing ◽  
Gene Encoding

scholarly journals Escherichia coli exonuclease VII. Cloning and sequencing of the gene encoding the large subunit (xseA).

1986 ◽  
Vol 261 (32) ◽  
pp. 14929-14935
Author(s):  
J W Chase ◽  
B A Rabin ◽  
J B Murphy ◽  
K L Stone ◽  
K R Williams
Keyword(s):  
Escherichia Coli ◽  
Large Subunit ◽  
Cloning And Sequencing ◽  
Gene Encoding ◽  
Exonuclease Vii

scholarly journals Regulation and Mechanism of Action of the Small Heat Shock Protein from the Hyperthermophilic ArchaeonPyrococcus furiosus

2001 ◽  
Vol 183 (17) ◽  
pp. 5198-5202 ◽  
Author(s):  
Pongpan Laksanalamai ◽  
Dennis L. Maeder ◽  
Frank T. Robb
Keyword(s):  
Escherichia Coli ◽  
Heat Shock ◽  
Heat Shock Protein ◽  
Mechanism Of Action ◽  
Pyrococcus Furiosus ◽  
Small Heat Shock Protein ◽  
Control Culture ◽  
Gene Encoding ◽  
E Coli

ABSTRACT The small heat shock protein (sHSP) from the hyperthermophilePyrococcus furiosus was specifically induced at the level of transcription by heat shock at 105°C. The gene encoding this protein was cloned and overexpressed in Escherichia coli. The recombinant sHSP prevented the majority of E. coli proteins from aggregating in vitro for up to 40 min at 105°C. The sHSP also prevented bovine glutamate dehydrogenase from aggregating at 56°C. Survivability of E. colioverexpressing the sHSP was enhanced approximately sixfold during exposure to 50°C for 2 h compared with the control culture, which did not express the sHSP. Apparently, the sHSP confers a survival advantage on mesophilic bacteria by preventing protein aggregation at supraoptimal temperatures.

scholarly journals Cloning and Sequencing of a Poly(dl-Lactic Acid) Depolymerase Gene from Paenibacillus amylolyticus Strain TB-13 and Its Functional Expression in Escherichia coli

2003 ◽  
Vol 69 (5) ◽  
pp. 2498-2504 ◽  
Author(s):  
Yukie Akutsu-Shigeno ◽  
Teerawat Teeraphatpornchai ◽  
Kamonluck Teamtisong ◽  
Nobuhiko Nomura ◽  
Hiroo Uchiyama ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Lactic Acid ◽  
Amino Acid ◽  
Functional Expression ◽  
Amino Acid Residues ◽  
Cloning And Sequencing ◽  
Gene Encoding ◽  
Butylene Succinate ◽  
Expression In Escherichia Coli ◽  
Poly Ethylene

ABSTRACT The gene encoding a poly(dl-lactic acid) (PLA) depolymerase from Paenibacillus amylolyticus strain TB-13 was cloned and overexpressed in Escherichia coli. The purified recombinant PLA depolymerase, PlaA, exhibited degradation activities toward various biodegradable polyesters, such as poly(butylene succinate), poly(butylene succinate-co-adipate), poly(ethylene succinate), and poly(ε-caprolactone), as well as PLA. The monomeric lactic acid was detected as the degradation product of PLA. The substrate specificity toward triglycerides and p-nitrophenyl esters indicated that PlaA is a type of lipase. The gene encoded 201 amino acid residues, including the conserved pentapeptide Ala-His-Ser-Met-Gly, present in the lipases of mesophilic Bacillus species. The identity of the amino acid sequence of PlaA with Bacillus lipases was no more than 45 to 50%, and some of its properties were different from those of these lipases.

Cloning and sequencing of the hemE gene encoding uroporphyrinogen III decarboxylase (UPD) from Escherichia coli K-12

Gene ◽  
1993 ◽  
Vol 133 (1) ◽  
pp. 109-113 ◽  
Author(s):  
Nishimura Koichi ◽  
Nakayashiki Toru ◽  
Inokuchi Hachiro
Keyword(s):  
Escherichia Coli ◽  
Cloning And Sequencing ◽  
Gene Encoding ◽  
K 12
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