Error-prone bypass of certain DNA lesions by the human DNA polymerase kappa

Article Abstract:

The human DNA polymerase kappa and its important error-prone bypass of certain DNA lesions are discussed in this research communication. The DinB protein of Escherichia coli is a recently identified error-prone DNA polymerase. A human homolog has been found and named DINB1. The DINB1 gene encodes a DNA polymerase called pol(kappa) and incorporates mismatched bases on an undamaged template often. It bypasses an abasic site and N-2-acetylaminofluorene-adduct in an error-prone way. The human DINB1 in a truncated form allows for the bypass.

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A multistep damage recognition mechanism for global genomic nucleotide excision repair

Article Abstract:

Damage recognition for nucleotide excision repair (NER) seems to require at least two steps. The multistep mechanism found may give a molecular basis for ensuring the high level of damage discrimination needed for global genomic NER. A detailed analysis of the binding specificity of the XPC-HR23B complex has been described with various DNA substrates used, each with one defined lesion. The XPC-HR23B complex, a mammalian NER factor, can bind specifically to certain DNA lesions and start the cell-free repair reaction. Additional factors and steps are likely neded for recognition of some kinds of lesions. Genetic aspects of xeroderma pigmentosum are discussed.

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DNA-binding polarity of human replication protein A positions nucleases in nucleotide excision repair

Article Abstract:

Affinity of human replication protein A (hRPA) for artificial DNA hairpin structures with 3' or 5' protruding single-stranded arms has been compared. Single-stranded DNA (ssDNA) is bound with a defined polarity by hRPA. The human ssDNA-binding replication A protein (RPA) has a role in assorted DNA-processing situations. Its DNA-binding polarity positions shows that nucleases are present in nucleotide excision repair with hRPA on the undamaged strand. It may be that the polarity of hRPA on ssDNA contributes to directionality of other processes dependent on hRPA.

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