High Fidelity Dna Replication In Mycobacterium Tuberculosis Relies On A

High Fidelity Dna Replication In Mycobacterium Tuberculosis Relies On A The polymerase and histidinol phosphatase (php) domain in the dna polymerase dnae1 is essential for mycobacterial high fidelity dna replication. Our work provides crucial insights into high fidelity dna replication in m. tuberculosis and reveals unique features of the php active site that can be exploited for development of new antibiotics to treat this major threat to global health.

High Fidelity Dna Replication In Mycobacterium Tuberculosis Relies On A High fidelity dna replication depends on a proofreading 3′–5′ exonuclease that is associated with the replicative dna polymerase. The replicative dna polymerase dnae1 from the major pathogen mycobacterium tuberculosis (mtb) uses its intrinsic php exonuclease that is distinct from the canonical dedd exonucleases found in the escherichia coli and eukaryotic replisomes. The replicative dna polymerase dnae1 from the major pathogen mycobacterium tuberculosis (mtb) uses its intrinsic php exonuclease that is distinct from the canonical dedd exonucleases found in the escherichia coli and eukaryotic replisomes. The polymerase and histidinol phosphatase (php) domain in the dna polymerase dnae1 is essential for mycobacterial high fidelity dna replication. here, the authors determine the dnae1 crystal structure, which reveals the php exonuclease mechanism that can be exploited for antibiotic development.

High Fidelity Dna Replication In Mycobacterium Tuberculosis Relies On A The replicative dna polymerase dnae1 from the major pathogen mycobacterium tuberculosis (mtb) uses its intrinsic php exonuclease that is distinct from the canonical dedd exonucleases found in the escherichia coli and eukaryotic replisomes. The polymerase and histidinol phosphatase (php) domain in the dna polymerase dnae1 is essential for mycobacterial high fidelity dna replication. here, the authors determine the dnae1 crystal structure, which reveals the php exonuclease mechanism that can be exploited for antibiotic development. Replication fidelity in mtb has been attributed mainly to the presence of the 3′–5′ exonuclease activity of dna polymerase dnae1 [2]. By analyzing the sequence polymorphism of dnaq in clinical isolates of mycobacterium tuberculosis (mtb), we demonstrated that a naturally evolved dnaq variant prevalent in mtb lineage 4.3 may enable hypermutability and is associated with drug resistance. The replicative dna polymerase dnae1 from the major pathogen mycobacterium tuberculosis (mtb) uses its intrinsic php exonuclease that is distinct from the canonical dedd exonucleases found in the escherichia coli and eukaryotic replisomes. The replicative dna polymerase dnae1 from the major pathogen mycobacterium tuberculosis (mtb) uses its intrinsic php exonuclease that is distinct from the canonical dedd exonucleases found in the escherichia coli and eukaryotic.