Structural insight into DNA joining: from conserved mechanisms to diverse scaffolds
| Autor: | Hanna-Kirsti S. Leiros, Adele Kim Williamson |
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| Rok vydání: | 2020 |
| Předmět: |
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Molecular chemistry.chemical_classification DNA ligase Genome VDP::Mathematics and natural science: 400::Chemistry: 440 DNA Ligases AcademicSubjects/SCI00010 Protein Conformation Mechanism (biology) Computational biology Multifunctional Enzymes Biology ENCODE Catalysis Structure-Activity Relationship chemistry.chemical_compound Protein structure chemistry VDP::Matematikk og Naturvitenskap: 400::Kjemi: 440 Genetics Humans Survey and Summary DNA |
| Zdroj: | Nucleic Acids Research |
| ISSN: | 1362-4962 0305-1048 |
| Popis: | DNA ligases are diverse enzymes with essential functions in replication and repair of DNA; here we review recent advances in their structure and distribution and discuss how this contributes to understanding their biological roles and technological potential. Recent high-resolution crystal structures of DNA ligases from different organisms, including DNA-bound states and reaction intermediates, have provided considerable insight into their enzymatic mechanism and substrate interactions. All cellular organisms possess at least one DNA ligase, but many species encode multiple forms some of which are modular multifunctional enzymes. New experimental evidence for participation of DNA ligases in pathways with additional DNA modifying enzymes is defining their participation in non-redundant repair processes enabling elucidation of their biological functions. Coupled with identification of a wealth of DNA ligase sequences through genomic data, our increased appreciation of the structural diversity and phylogenetic distribution of DNA ligases has the potential to uncover new biotechnological tools and provide new treatment options for bacterial pathogens. |
| Databáze: | OpenAIRE |
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