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Published on: November 28, 2012
Interaction of DNA with bovine lens alpha-crystallin: its functional implications
K Singh1, B Groth-Vasselli, P N Farnsworth
1Department of Biochemistry and Molecular Biology, UMD, New Jersey Medical School, Newark 07103, USA.
Abstract:
Under normal conditions, lens aggregates of alpha-crystallin subunits, alpha A and alpha B, are found in the cytoplasm. However, during stress in nonlenticular tissues, alpha B translocates to the nucleus. A sequence study revealed that both subunits share a consensus sequence with other DNA binding proteins. These observations prompted us to investigate DNA binding with alpha-crystallin by UV-mediated photo-crosslinking. The data show that both single and double stranded DNA crosslink mainly with tetramers of alpha-crystallin subunits. The formation of tetramers appears to modify alpha-crystallin interactive properties and, therefore, its induction may have functional significance. These observations suggest that alpha-crystallin may have a nuclear function which includes DNA binding.
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