Architecture of Y-Family DNA Polymerases Relevant to Translesion DNA Synthesis as Revealed in Structural and Molecular Modeling StudiesReportar como inadecuado


Architecture of Y-Family DNA Polymerases Relevant to Translesion DNA Synthesis as Revealed in Structural and Molecular Modeling Studies


Architecture of Y-Family DNA Polymerases Relevant to Translesion DNA Synthesis as Revealed in Structural and Molecular Modeling Studies - Descarga este documento en PDF. Documentación en PDF para descargar gratis. Disponible también para leer online.

Citation

Chandani, Sushil, Christopher Jacobs, Edward L. Loechler. -Architecture of Y-Family DNA Polymerases Relevant to Translesion DNA Synthesis as Revealed in Structural and Molecular Modeling Studies- Journal of Nucleic Acids 2010:784081.

Abstract

DNA adducts, which block replicative DNA polymerases DNAPs, are often bypassed by lesion-bypass DNAPs, which are mostly in the Y-Family. Y-Family DNAPs can do non-mutagenic or mutagenic dNTP insertion, and understanding this difference is important, because mutations transform normal into tumorigenic cells. Y-Family DNAP architecture that dictates mechanism, as revealed in structural and modeling studies, is considered. Steps from adduct blockage of replicative DNAPs, to bypass by a lesion-bypass DNAP, to resumption of synthesis by a replicative DNAP are described. Catalytic steps and protein conformational changes are considered. One adduct is analyzed in greater detail: the major benzoapyrene adduct BaP-N2-dG, which is bypassed non-mutagenically dCTP insertion by Y-family DNAPs in the IV-κ-class and mutagenically dATP insertion by V-η-class Y-Family DNAPs. Important architectural differences between IV-κ-class versus V-η-class DNAPs are discussed, including insights gained by analyzing ~400 sequences each for bacterial DNAPs IV and V, along with sequences from eukaryotic DNAPs kappa, eta and iota. The little finger domains of Y-Family DNAPs do not show sequence conservation; however, their structures are remarkably similar due to the presence of a core of hydrophobic amino acids, whose exact identity is less important than the hydrophobic amino acid spacing.Rights

Copyright 2010 Sushil Chandani et al.

CAS: Biology: Scholarly Papers - ENG: Bioinformatics: Scholarly Papers -



Autor: Chandani, Sushil - Jacobs, Christopher - Loechler, Edward L. - -

Fuente: https://open.bu.edu/







Documentos relacionados