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Oligomerization of site-specific nicking endonuclease BspD6I at high protein concentrations

The ability of site-specific nicking endonuclease BspD6I (Nt.BspD6I) to oligomerize at concentrations > 0.5 μM (>0.035 mg/mL) is studied. Three states of Nt.BspD6I are registered via electrophoretic studies both in the presence and in the absence of DNA. Estimation of their molecular mass allo...

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Published in:	Russian journal of bioorganic chemistry 2012-07, Vol.38 (4), p.376-382
Main Authors:	Sekerina, S. A., Grishin, A. V., Ryazanova, A. Yu, Artyukh, R. I., Rogulin, E. A., Yunusova, A. K., Oretskaya, T. S., Zheleznaya, L. A., Kubareva, E. A.
Format:	Article
Language:	English
Subjects:	Biochemistry Biomedical and Life Sciences Biomedicine Bioorganic Chemistry DNA Electrostatic properties Endonuclease Life Sciences Monomers Nicking Oligomerization Organic Chemistry Protein interaction
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container_title	Russian journal of bioorganic chemistry
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creator	Sekerina, S. A. Grishin, A. V. Ryazanova, A. Yu Artyukh, R. I. Rogulin, E. A. Yunusova, A. K. Oretskaya, T. S. Zheleznaya, L. A. Kubareva, E. A.
description	The ability of site-specific nicking endonuclease BspD6I (Nt.BspD6I) to oligomerize at concentrations > 0.5 μM (>0.035 mg/mL) is studied. Three states of Nt.BspD6I are registered via electrophoretic studies both in the presence and in the absence of DNA. Estimation of their molecular mass allows assigning them as a monomer, a dimer and a trimer. Both dimeric and monomeric Nt.BspD6I are shown to hydrolyze its DNA substrate with the same specificity. Calculation of the electrostatic potential distribution on the Nt.BspD6I globule surface shows that the protein molecule is a dipole. The Nt.BspD6I oligomeric forms are likely to be the result of ionic protein-protein interactions.
doi_str_mv	10.1134/S1068162012040127
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Both dimeric and monomeric Nt.BspD6I are shown to hydrolyze its DNA substrate with the same specificity. Calculation of the electrostatic potential distribution on the Nt.BspD6I globule surface shows that the protein molecule is a dipole. The Nt.BspD6I oligomeric forms are likely to be the result of ionic protein-protein interactions.</description><subject>Biochemistry</subject><subject>Biomedical and Life Sciences</subject><subject>Biomedicine</subject><subject>Bioorganic Chemistry</subject><subject>DNA</subject><subject>Electrostatic properties</subject><subject>Endonuclease</subject><subject>Life Sciences</subject><subject>Monomers</subject><subject>Nicking</subject><subject>Oligomerization</subject><subject>Organic Chemistry</subject><subject>Protein interaction</subject><issn>1068-1620</issn><issn>1608-330X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2012</creationdate><recordtype>article</recordtype><recordid>eNp9UD1PwzAQtRBIlMIPYPPIEvDZjZ2MUL4qVeoASEgMkXtxWpfUDnYywK_HpWxILHcnvQ_de4ScA7sEEJOrJ2CyAMkZcDZJQx2QEUhWZEKw18N0Jzjb4cfkJMYNY8BYXozI26K1K781wX7p3npHfUOj7U0WO4O2sUidxXfrVtS42rsBW6OjoTexu5Uzqnu6tqs17YLvjXUUvUPj-vBjFU_JUaPbaM5-95i83N89Tx-z-eJhNr2eZyg49NlEqlIwxkHXugS51FLzOpdYCwWoS8VKk0KggBwLqZdalQprLGqmGs615GJMLva-6Y2PwcS-2tqIpm21M36IFYCCQvEcdlTYUzH4GINpqi7YrQ6fFbBqV2T1p8ik4XtNTFy3MqHa-CG4lOgf0TdXwnUz</recordid><startdate>20120701</startdate><enddate>20120701</enddate><creator>Sekerina, S. 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subjects	Biochemistry Biomedical and Life Sciences Biomedicine Bioorganic Chemistry DNA Electrostatic properties Endonuclease Life Sciences Monomers Nicking Oligomerization Organic Chemistry Protein interaction
title	Oligomerization of site-specific nicking endonuclease BspD6I at high protein concentrations
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