A Protein Related to Eucaryal and Bacterial DNA-Motor Proteins in the Hyperthermophilic Archaeon Sulfolobus acidocaldarius |
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Authors: | Christiane Elie Marie- France Baucher Christian Fondrat Patrick Forterre |
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Institution: | (1) Laboratoire de Biologie Moléculaire des Extrêmophiles, Institut de Génétique et Microbiologie, CNRS, URA 1354. Bat. 409. Université Paris-Sud, 91405 Orsay cedex, France, FR;(2) CITI2. Centre InterUniversitaire d'Informatique à Orientation Biomédicale, 45 rue des Saint-Pères, 75270 Paris Cedex 06, France, FR |
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Abstract: | We have isolated a new gene encoding a putative 103-kDa protein from the hyperthermophilic archaeon Sulfolobus acidocaldarius. Analysis of the deduced amino-acid sequence shows an extended central domain, predicted to form coiled-coil structures, and
two terminal domains that display purine NTPase motifs. These features are reminiscent of mechanochemical motor proteins which
use the energy of ATP hydrolysis to move specific cellular components. Comparative analysis of the amino-acid sequence of
the terminal domains and predicted structural organization of this putative purine NTPase show that it is related both to
eucaryal proteins from the ``SMC family' involved in the condensation of chromosomes and to several bacterial and eucaryal
proteins involved in DNA recombination/repair. Further analyses revealed that these proteins are all members of the so called
``UvrA-related NTP-binding proteins superfamily' and form a large subgroup of motor-like NTPases involved in different DNA
processing mechanisms. The presence of such protein in Archaea, Bacteria, and Eucarya suggests an early origin of DNA-motor
proteins that could have emerged and diversified by domain shuffling.
Received: 29 June 1996 / Accepted: 28 February 1997 |
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Keywords: | : Hyperthermophilic archaea — Sulfolobus acidocaldarius— Purine NTPase — Coiled-coil structures — DNA-motor proteins — SMC-like proteins — UvrA-related proteins — Domain shuffling |
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