The hyperthermophilic archaeon Pyrococcus furiosus utilizes environmental iron sulfide cluster complexes as an iron source

Extremophiles ◽  
2021 ◽  
Author(s):  
Sonya M. Clarkson ◽  
Dominik K. Haja ◽  
Michael W. W. Adams
2010 ◽  
Vol 192 (21) ◽  
pp. 5841-5843 ◽  
Author(s):  
Sonya M. Clarkson ◽  
Elizabeth C. Newcomer ◽  
Everett G. Young ◽  
Michael W. W. Adams

ABSTRACT The gene (sipA) encoding the sulfur-induced protein A (PF2025) is highly upregulated during growth of Pyrococcus furiosus on elemental sulfur (S0). Expression of sipA is regulated by sulfide, the product of S0 reduction, but in an iron-dependent manner. SipA is proposed to play a role in intracellular iron sulfide detoxification.


1998 ◽  
Vol 180 (8) ◽  
pp. 2232-2236 ◽  
Author(s):  
Yoshizumi Ishino ◽  
Kayoko Komori ◽  
Isaac K. O. Cann ◽  
Yosuke Koga

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.


PLoS ONE ◽  
2013 ◽  
Vol 8 (3) ◽  
pp. e58497 ◽  
Author(s):  
Kazuo Tori ◽  
Sonoko Ishino ◽  
Shinichi Kiyonari ◽  
Saki Tahara ◽  
Yoshizumi Ishino

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