MersV1, Main, Exploration, bibRecord, 003D90

Annealing of complementary DNA strands above the melting point of the duplex promoted by an archaeal protein

Identifieur interne : 003D90 ( Main/Exploration ); précédent : 003D89; suivant : 003D91

Annealing of complementary DNA strands above the melting point of the duplex promoted by an archaeal protein

Auteurs : Annamaria Guagliardi [Italie] ; Alessandra Napoli [Italie] ; Mosé Rossi [Italie] ; Maria Ciaramella [Italie]

Source :

Journal of Molecular Biology [ 0022-2836 ] ; 1997.

RBID : ISTEX:31DE31A514D00EDAD7391ED88441183477A7EFB2

English descriptors

KwdEn :
- Archaea, DNA annealing, DNA binding protein, ds, homologous pairing, ss, thermophiles, tm.
Teeft :
- Acad, Annealing, Annealing activity, Annealing reaction, Archaebacterium, Assay, Baumann, Biol, Chromosomal protein, Complementary, Double helix, Duplex, Escherichia coli, High temperature, Independent experiments, Mismatch, Naked probe, Natl, Natl acad, Oligonucleotide, Oligonucleotides, Proc, Reaction conditions, Reca, Reca protein, Recombination, Reddy suryanarayana, Renaturation, Renaturation activity, Renaturation reaction, Solfataricus, Sso7d, Standard reactions, Sulfolobus, Unpublished results.

Abstract

Abstract: One enigma in the biology of hyperthermophilic microorganisms, living near or above 100°C, is how their genomes can be stable and, at the same time, plastic at temperatures above the melting point. The non-specific DNA-binding protein Sso7d of the hyperthermophilic archaeon Sulfolobus solfataricus is known to protect DNA from thermal denaturation. We report here that Sso7d promotes the renaturation of complementary DNA strands at temperatures above the melting point of the duplex. This novel annealing activity is strictly homology-dependent, and even one mismatch in a stretch of 17 complementary bases severely reduces its efficiency. Since pairing of homologous single strands is a key step in all fundamental processes involving nucleic acids, such as transcription, replication, recombination, and repair, Sso7d is a candidate component of the protein machinery devoted to the coupling of DNA stability to metabolic flexibility at high temperature.

Url:

https://api.istex.fr/ark:/67375/6H6-R0FFSJLT-3/fulltext.pdf

DOI: 10.1006/jmbi.1996.0873

Affiliations:

Italie

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Le document en format XML

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<front><div type="abstract" xml:lang="en">Abstract: One enigma in the biology of hyperthermophilic microorganisms, living near or above 100°C, is how their genomes can be stable and, at the same time, plastic at temperatures above the melting point. The non-specific DNA-binding protein Sso7d of the hyperthermophilic archaeon Sulfolobus solfataricus is known to protect DNA from thermal denaturation. We report here that Sso7d promotes the renaturation of complementary DNA strands at temperatures above the melting point of the duplex. This novel annealing activity is strictly homology-dependent, and even one mismatch in a stretch of 17 complementary bases severely reduces its efficiency. Since pairing of homologous single strands is a key step in all fundamental processes involving nucleic acids, such as transcription, replication, recombination, and repair, Sso7d is a candidate component of the protein machinery devoted to the coupling of DNA stability to metabolic flexibility at high temperature.</div>
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Annealing of complementary DNA strands above the melting point of the duplex promoted by an archaeal protein

Annealing of complementary DNA strands above the melting point of the duplex promoted by an archaeal protein

Source :

English descriptors

Abstract

Links toward previous steps (curation, corpus...)

Le document en format XML

Pour manipuler ce document sous Unix (Dilib)

Pour mettre un lien sur cette page dans le réseau Wicri