Chemical modifications of actin: effects on interaction with deoxyribonuclease I |
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| Authors: | Joan S.Y. Ng Leslie D. Burtnick |
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| Affiliation: | Department of Chemistry, University of British Columbia, Vancouver, British Columbia Canada V6T 1Y6 |
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| Abstract: | Maleylation of lysine residues, nitration of tyrosine residues or modification with 2,3-butanedione or 1,2-cyclohexanedione of arginine residues on actin resulted in a loss of polymerizability of the modified actin. However, only lysine modification produced a complete loss of the deoxyribunuclease I inhibitory ability of actin at low degrees of modification. By the level of one modified lysine per actin monomer, the samples completely lost polymerizability and lost 65% of their inhibitory power against deoxyribonuclease I-catalysed hydrolysis of DNA. By two lysines modified per actin, all inhibitory activity was lost. One lysine residue on actin apparently overlaps both an actin action contact site and an actin-deoxyribnuclease 1 contact site, offering a suggestion as to how deoxyribonuclease I blocks actin polymerization. |
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| Keywords: | Polymerization actin chemical modification binding of DNase I DNase I deoxyribonuclease I, EC 3.1.4.5 DTT dithiothereitol DTNB 5,5′-dithiobis(2-nitobenzoic acid) BD 2,3-butanedione CD 1,2′-cyclohexxanedione TNM tetranitromethane buffer A buffer B To whom correspondence should be addressed. |
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