Community analysis of a mercury hot spring supports occurrence of domain-specific forms of mercuric reductase

Jessica Simbahan, Elizabeth Kurth, James Schelert, Amanda Dillman, Etsuko Moriyama, Stevan Jovanovich, Paul Blum

Research output: Contribution to journalArticle

36 Citations (Scopus)

Abstract

Mercury is a redox-active heavy metal that reacts with active thiols and depletes cellular antioxidants. Active resistance to the mercuric ion is a widely distributed trait among bacteria and results from the action of mercuric reductase (MerA). Protein phylogenetic analysis of MerA in bacteria indicated the occurrence of a second distinctive form of MerA among the archaea, which lacked an N-terminal metal recruitment domain and a C-terminal active tyrosine. To assess the distribution of the forms of MerA in an interacting community comprising members of both prokaryotic domains, studies were conducted at a naturally occurring mercury-rich geothermal environment. Geochemical analyses of Coso Hot Springs indicated that mercury ore (cinnabar) was present at concentrations of parts per thousand. Under high-temperature and acid conditions, cinnabar may be oxidized to the toxic form Hg2+, necessitating mercury resistance in resident prokaryotes. Culture-independent analysis combined with culture-based methods indicated the presence of thermophilic crenarchaeal and gram-positive bacterial taxa. Fluorescence in situ hybridization analysis provided quantitative data for community composition. DNA sequence analysis of archaeal and bacterial merA sequences derived from cultured pool isolates and from community DNA supported the hypothesis that both forms of MerA were present. Competition experiments were performed to assess the role of archaeal merA in biological fitness. An essential role for this protein was evident during growth in a mercury-contaminated environment. Despite environmental selection for mercury resistance and the proximity of community members, MerA retains the two distinct prokaryotic forms and avoids genetic homogenization.

Original languageEnglish (US)
Pages (from-to)8836-8845
Number of pages10
JournalApplied and environmental microbiology
Volume71
Issue number12
DOIs
StatePublished - Dec 1 2005

Fingerprint

Hot Springs
hot springs
thermal spring
Mercury
mercury
cinnabar
Bacteria
DNA
bacterium
protein
thiol
Poisons
prokaryote
Archaea
bacteria
prokaryotic cells
homogenization
Heavy Metals
fluorescence in situ hybridization
thiols

ASJC Scopus subject areas

  • Biotechnology
  • Food Science
  • Applied Microbiology and Biotechnology
  • Ecology

Cite this

Community analysis of a mercury hot spring supports occurrence of domain-specific forms of mercuric reductase. / Simbahan, Jessica; Kurth, Elizabeth; Schelert, James; Dillman, Amanda; Moriyama, Etsuko; Jovanovich, Stevan; Blum, Paul.

In: Applied and environmental microbiology, Vol. 71, No. 12, 01.12.2005, p. 8836-8845.

Research output: Contribution to journalArticle

Simbahan, Jessica ; Kurth, Elizabeth ; Schelert, James ; Dillman, Amanda ; Moriyama, Etsuko ; Jovanovich, Stevan ; Blum, Paul. / Community analysis of a mercury hot spring supports occurrence of domain-specific forms of mercuric reductase. In: Applied and environmental microbiology. 2005 ; Vol. 71, No. 12. pp. 8836-8845.
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