Interaction of DNA with bovine lens alpha-crystallin: its functional implications.
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.
Singh
K
K
Department of Biochemistry and Molecular Biology, UMD, New Jersey Medical School, Newark 07103, USA.
Groth-Vasselli
B
B
Farnsworth
P N
PN
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D002417:Cattle; D002467:Cell Nucleus / Q000378:metabolism; D003432:Cross-Linking Reagents; D003459:Crystallins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D003593:Cytoplasm / Q000378:metabolism; D004247:DNA / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D066298:In Vitro Techniques; D007908:Lens, Crystalline / Q000737:chemistry / Q000378:metabolism; D046911:Macromolecular Substances; D008969:Molecular Sequence Data; D011485:Protein Binding; D011487:Protein Conformation; D017433:Protein Structure, Secondary / Q000528:radiation effects; D017386:Sequence Homology, Amino Acid; D014466:Ultraviolet Rays
D003432:Cross-Linking Reagents; D003459:Crystallins; D046911:Macromolecular Substances; D004247:DNA