Understanding the evolution of restriction-modification systems: Clues from sequence and structure comparisons

• Autorzy: Bujnicki J. M.
• Języki publikacji: EN

Abstrakty

EN

Restriction-modification (RM) systems comprise two opposing enzymatic activities: a restriction endonuclease, that targets specific DNA sequences and performs endonucleolytic cleavage, and a modification methyltransferase that renders these se­quences resistant to cleavage. Studies on molecular genetics and biochemistry of RM systems have been carried out over the past four decades, laying foundations for mod­ern molecular biology and providing important models for mechanisms of highly spe­cific protein-DNA interactions. Although the number of known, relevant sequences 3D structures of RM proteins is growing steadily, we do not fully understand their functional diversities from an evolutionary perspective and we are not yet able to en­gineer new sequence specificities based on rational approaches. Recent findings on the evolution of RM systems and on their structures and mechanisms of action have led to a picture in which conserved modules with defined function are shared between different RM proteins and other enzymes involved in nucleic acid biochemistry. On the other hand, it has been realized that some of the modules have been replaced in the evolution by unrelated domains exerting similar function. The aim of this review is to give a survey on the recent progress in the field of structural phylogeny of RM en­zymes with special emphasis on studies of sequence-structure-function relationships and emerging potential applications in biotechnology.

Słowa kluczowe

EN

methyltransferase; molecular evolution; enzyme activity; protein structure; evolution; endonuclease

• Wydawca: -
• Czasopismo: Acta Biochimica Polonica
• Rocznik: 2001
• Tom: 48
• Numer: 4
• Opis fizyczny: p.935-967,fig.

Twórcy

autor

Bujnicki J. M.

• BioInfoBank Institute, Limanowskiego 24A, 60-744 Poznan, Poland

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