On the mineral core of ferritin-like proteins: structural and magnetic characterization

We report a combined structural and magnetic study of the mineral core biomineralized by horse spleen ferritin and three prokaryotic ferritin-like proteins: bacterial ferritin and bacterioferritin from Escherichia coli and archaeal ferritin from Pyrococcus furiosus.

Download Full-text

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

Gene ◽

10.1016/0378-1119(95)00128-s ◽

1995 ◽

Vol 160 (1) ◽

pp. 101-103 ◽

Cited By ~ 2

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

Download Full-text

Analyzing the binding of Co(II)-specific inhibitors to the methionyl aminopeptidases from Escherichia coli and Pyrococcus furiosus

JBIC Journal of Biological Inorganic Chemistry ◽

10.1007/s00775-009-0471-2 ◽

2009 ◽

Vol 14 (4) ◽

pp. 573-585 ◽

Cited By ~ 6

Author(s):

Sanghamitra Mitra ◽

George Sheppard ◽

Jieyi Wang ◽

Brian Bennett ◽

Richard C. Holz

Keyword(s):

Escherichia Coli ◽

Pyrococcus Furiosus ◽

Specific Inhibitors

Download Full-text

A Novel DNA Polymerase Family Found inArchaea

Journal of Bacteriology ◽

10.1128/jb.180.8.2232-2236.1998 ◽

1998 ◽

Vol 180 (8) ◽

pp. 2232-2236 ◽

Cited By ~ 69

Author(s):

Yoshizumi Ishino ◽

Kayoko Komori ◽

Isaac K. O. Cann ◽

Yosuke Koga

Keyword(s):

Escherichia Coli ◽

Dna Polymerase ◽

Pyrococcus Furiosus ◽

Dna Polymerases ◽

Open Reading Frames ◽

Gene Products ◽

Polymerase Gene ◽

Hyperthermophilic Archaeon ◽

Dna Polymerase Ii ◽

Reading Frames

ABSTRACT One of the most puzzling results from the complete genome sequence of the methanogenic archaeon Methanococcus jannaschii was that the organism may have only one DNA polymerase gene. This is because no other DNA polymerase-like open reading frames (ORFs) were found besides one ORF having the typical α-like DNA polymerase (family B). Recently, we identified the genes of DNA polymerase II (the second DNA polymerase) from the hyperthermophilic archaeonPyrococcus furiosus, which has also at least one α-like DNA polymerase (T. Uemori, Y. Sato, I. Kato, H. Doi, and Y. Ishino, Genes Cells 2:499–512, 1997). The genes in M. jannaschiiencoding the proteins that are homologous to the DNA polymerase II ofP. furiosus have been located and cloned. The gene products of M. jannaschii expressed in Escherichia colihad both DNA polymerizing and 3′→5′ exonuclease activities. We propose here a novel DNA polymerase family which is entirely different from other hitherto-described DNA polymerases.

Download Full-text

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

Journal of Bacteriology ◽

10.1128/jb.183.17.5198-5202.2001 ◽

2001 ◽

Vol 183 (17) ◽

pp. 5198-5202 ◽

Cited By ~ 41

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.

Download Full-text