Polypeptide synthesis on ribosomes of an extreme thermophilic hydrogen bacterium Calderobacterium hydrogenophilum

Mikulı́k, Karel; Jiráňová, Anna; Mañas, Juan Manuel González; Spížek, J.; Anděra, Ladislav; Savelyeva, Nadja D.

doi:10.1007/bf00249076

Cited by 5 publications

(1 citation statement)

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“…In this communication, we describe the purification and properties of reverse gyrase from the extremely thermophilic, hydrogen-oxidizing eubacterium Calderobacterium hydrogenophilum [13]. C. hydrogenophilum was classified as a eubacterium for its eubacterial type of ribosomes [14]. It also contains DNA-dependent RNA polymerase with the eubacterial-like composition of its major subunits [15].…”

Section: Introductionmentioning

confidence: 99%

Characterization of a reverse gyrase from the extremely thermophilic hydrogen-oxidizing eubacterium Calderobacterium hydrogenophilum

Andera¹

1993

FEMS Microbiology Letters

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Reverse gyrase was isolated from an extremely thermophilic hydrogen‐oxidizing eubacterium Calderobacterium hydrogenophilum. The enzyme catalyses the introduction of positive supercoils into the covalent closed DNA and requires ATP or dATP for its activity. So far, reverse gyrase has been purified to homogeneity only from thermophilic archaebacteria. Reverse gyrase from C. hydrogenophilum such as the archaebacterial enzymes is a monomeric protein and has a molecular mass between 115 and 120 kDa. The optimal reaction temperature is 90°C and the thermostability of this reverse gyrase is remarkable. The enzyme retains more than 95% of the activity after 40 min of incubation at 100°C.

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Section: Introductionmentioning

confidence: 99%