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At each step along this coordinate, the enzyme must form DNA interactions that are highly specialized for either rapid damage searching or catalysis.
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Plasma citrulline concentration, plasma I-FABP (biomarker of enterocyte damage), search for sepsis, results of bacterial sample, and usual clinical and biological variables were collected.
The experiments are designed to shed more light onto specific parameters that are currently proposed to govern damage search and recognition by endonucleases III.
Comparisons of these models with biochemical nicking data revealed significant changes in the damage search mechanisms between wild-type pdgs and most of the mutant enzymes.
The implications of these findings to the damage search process in human cells are discussed.
These findings provide key insights into how the ionic environment in cells influences the DNA damage search pathway.
In this study, we use CC theory to understand how each transient complex on the damage search pathway of human uracil DNA glycosylase (hUNG) responds to changes in salt concentration.
Since most studies of the damage search mechanism have used dilute, low-salt solutions, a key unknown is how the individual nonspecific and specific complexes respond to the high salt concentrations encountered in the cell nucleus.
This process begins with diffusion-controlled engagement of undamaged DNA, followed by a damage search step in which the enzyme remains loosely associated with the DNA chain (translocation), and finally, a recognition step that allows the enzyme to efficiently bind and excise uracil when it is encountered.
It is generally accepted that the DNA glycosylase damage search process involves two major modes: an associative a mode that involves tracking along the DNA using a loosely associated enzyme state (often called "sliding") and a dissociative mode that involves intermittent dissociation and reassociation of the enzyme with the DNA chain ("hopping").
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