The herpes simplex virus type-1 origin binding protein. DNA helicase activity
The herpes simplex virus type 1 (HSV-1) origin binding protein, the product of the UL9 gene, catalyzes the unwinding of DNA in the 3'-5' direction. Helicase activity is coupled to the hydrolysis of ATP or dATP and to a lesser extent to CTP, dCTP, or UTP. It requires a divalent cation (Mg2+...
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| Veröffentlicht in: | The Journal of biological chemistry 1993-01, Vol.268 (2), p.1220-1225 |
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| container_title | The Journal of biological chemistry |
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| creator | BOEHMER, P. E DODSON, M. S LEHMAN, I. R |
| description | The herpes simplex virus type 1 (HSV-1) origin binding protein, the product of the UL9 gene, catalyzes the unwinding of DNA
in the 3'-5' direction. Helicase activity is coupled to the hydrolysis of ATP or dATP and to a lesser extent to CTP, dCTP,
or UTP. It requires a divalent cation (Mg2+ > Mn2+ > Ca2+) with an optimum at 2.5 mM MgCl2. Activity is optimal at high pH
(8.5-9.5) and high temperature (45 degrees C) and is inhibited at ionic strengths > 50 mM NaCl. The helicase activity is specifically
stimulated by the HSV-1-encoded single-stranded DNA-binding protein, ICP8, which increases both the rate and extent of helicase
activity. Helicase action appears to be stoichiometric, requiring a DNA-dependent assembly of a multimeric UL9 protein complex.
Under optimal conditions, the rate of DNA unwinding is approximately 75 base pairs/min. |
| doi_str_mv | 10.1016/S0021-9258(18)54063-1 |
| format | Article |
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in the 3'-5' direction. Helicase activity is coupled to the hydrolysis of ATP or dATP and to a lesser extent to CTP, dCTP,
or UTP. It requires a divalent cation (Mg2+ > Mn2+ > Ca2+) with an optimum at 2.5 mM MgCl2. Activity is optimal at high pH
(8.5-9.5) and high temperature (45 degrees C) and is inhibited at ionic strengths > 50 mM NaCl. The helicase activity is specifically
stimulated by the HSV-1-encoded single-stranded DNA-binding protein, ICP8, which increases both the rate and extent of helicase
activity. Helicase action appears to be stoichiometric, requiring a DNA-dependent assembly of a multimeric UL9 protein complex.
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in the 3'-5' direction. Helicase activity is coupled to the hydrolysis of ATP or dATP and to a lesser extent to CTP, dCTP,
or UTP. It requires a divalent cation (Mg2+ > Mn2+ > Ca2+) with an optimum at 2.5 mM MgCl2. Activity is optimal at high pH
(8.5-9.5) and high temperature (45 degrees C) and is inhibited at ionic strengths > 50 mM NaCl. The helicase activity is specifically
stimulated by the HSV-1-encoded single-stranded DNA-binding protein, ICP8, which increases both the rate and extent of helicase
activity. Helicase action appears to be stoichiometric, requiring a DNA-dependent assembly of a multimeric UL9 protein complex.
Under optimal conditions, the rate of DNA unwinding is approximately 75 base pairs/min.</description><subject>Base Composition</subject><subject>Base Sequence</subject><subject>Biological and medical sciences</subject><subject>Cations, Divalent</subject><subject>DNA Helicases - genetics</subject><subject>DNA Helicases - metabolism</subject><subject>DNA-Binding Proteins - genetics</subject><subject>DNA-Binding Proteins - metabolism</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Genes, Viral</subject><subject>herpes simplex virus 1</subject><subject>Kinetics</subject><subject>Molecular and cellular biology</subject><subject>Molecular genetics</subject><subject>Molecular Sequence Data</subject><subject>Nucleotides - pharmacology</subject><subject>Oligodeoxyribonucleotides</subject><subject>Replication</subject><subject>Simplexvirus - enzymology</subject><subject>Simplexvirus - genetics</subject><subject>Substrate Specificity</subject><subject>Viral Proteins - genetics</subject><subject>Viral Proteins - metabolism</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1993</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkE1PGzEQhi3UCsLHT0CyUFW1hwWPPzazR0RLW4nCoTn0ZnkdO2u0X9gbSv59DYlyZQ4eyfO8Y-sh5BzYJTAor_4wxqGouMIvgF-VZKUo4IDMgKEohIK_H8hsjxyR45QeWS5ZwSE5RIFMMpyR34vG0cbF0SWaQje27oU-h7hOdNqMrgA6xLAKPa1Dvwz9io5xmFzoL-m3--uca4M1yVFjp_Acps0p-ehNm9zZrp-Qxe33xc3P4u7hx6-b67vCSoFTYbj3pVQCjZyDZFY6iR44SvBW5lNVUJf5cslZ5WvESrGlNbaaA6KXRpyQz9u1-TdPa5cm3YVkXdua3g3rpOdKiYqhfBeEUgqmkGdQbUEbh5Si83qMoTNxo4HpV936Tbd-dakB9ZtuDTl3vntgXXduuU_t_Ob5p93cJGtaH01vQ9pjUpXIS5Wxiy3WhFXzL0Sn6zDYxnWal6i5Bs6Z-A8ohpF_</recordid><startdate>19930115</startdate><enddate>19930115</enddate><creator>BOEHMER, P. E</creator><creator>DODSON, M. S</creator><creator>LEHMAN, I. R</creator><general>American Society for Biochemistry and Molecular Biology</general><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7TM</scope><scope>7U9</scope><scope>H94</scope><scope>7X8</scope></search><sort><creationdate>19930115</creationdate><title>The herpes simplex virus type-1 origin binding protein. DNA helicase activity</title><author>BOEHMER, P. E ; DODSON, M. S ; LEHMAN, I. R</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c438t-a2ff64538a47140c4e48f12841fc4841591b64e4d209fb88950dcac97188f4a3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1993</creationdate><topic>Base Composition</topic><topic>Base Sequence</topic><topic>Biological and medical sciences</topic><topic>Cations, Divalent</topic><topic>DNA Helicases - genetics</topic><topic>DNA Helicases - metabolism</topic><topic>DNA-Binding Proteins - genetics</topic><topic>DNA-Binding Proteins - metabolism</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Genes, Viral</topic><topic>herpes simplex virus 1</topic><topic>Kinetics</topic><topic>Molecular and cellular biology</topic><topic>Molecular genetics</topic><topic>Molecular Sequence Data</topic><topic>Nucleotides - pharmacology</topic><topic>Oligodeoxyribonucleotides</topic><topic>Replication</topic><topic>Simplexvirus - enzymology</topic><topic>Simplexvirus - genetics</topic><topic>Substrate Specificity</topic><topic>Viral Proteins - genetics</topic><topic>Viral Proteins - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>BOEHMER, P. E</creatorcontrib><creatorcontrib>DODSON, M. S</creatorcontrib><creatorcontrib>LEHMAN, I. R</creatorcontrib><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Nucleic Acids Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>The Journal of biological chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>BOEHMER, P. E</au><au>DODSON, M. S</au><au>LEHMAN, I. R</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The herpes simplex virus type-1 origin binding protein. DNA helicase activity</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>1993-01-15</date><risdate>1993</risdate><volume>268</volume><issue>2</issue><spage>1220</spage><epage>1225</epage><pages>1220-1225</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><coden>JBCHA3</coden><abstract>The herpes simplex virus type 1 (HSV-1) origin binding protein, the product of the UL9 gene, catalyzes the unwinding of DNA
in the 3'-5' direction. Helicase activity is coupled to the hydrolysis of ATP or dATP and to a lesser extent to CTP, dCTP,
or UTP. It requires a divalent cation (Mg2+ > Mn2+ > Ca2+) with an optimum at 2.5 mM MgCl2. Activity is optimal at high pH
(8.5-9.5) and high temperature (45 degrees C) and is inhibited at ionic strengths > 50 mM NaCl. The helicase activity is specifically
stimulated by the HSV-1-encoded single-stranded DNA-binding protein, ICP8, which increases both the rate and extent of helicase
activity. Helicase action appears to be stoichiometric, requiring a DNA-dependent assembly of a multimeric UL9 protein complex.
Under optimal conditions, the rate of DNA unwinding is approximately 75 base pairs/min.</abstract><cop>Bethesda, MD</cop><pub>American Society for Biochemistry and Molecular Biology</pub><pmid>8380408</pmid><doi>10.1016/S0021-9258(18)54063-1</doi><tpages>6</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | The Journal of biological chemistry, 1993-01, Vol.268 (2), p.1220-1225 |
| issn | 0021-9258 1083-351X |
| language | eng |
| recordid | cdi_proquest_miscellaneous_75539084 |
| source | MEDLINE; Alma/SFX Local Collection; EZB Electronic Journals Library |
| subjects | Base Composition Base Sequence Biological and medical sciences Cations, Divalent DNA Helicases - genetics DNA Helicases - metabolism DNA-Binding Proteins - genetics DNA-Binding Proteins - metabolism Fundamental and applied biological sciences. Psychology Genes, Viral herpes simplex virus 1 Kinetics Molecular and cellular biology Molecular genetics Molecular Sequence Data Nucleotides - pharmacology Oligodeoxyribonucleotides Replication Simplexvirus - enzymology Simplexvirus - genetics Substrate Specificity Viral Proteins - genetics Viral Proteins - metabolism |
| title | The herpes simplex virus type-1 origin binding protein. DNA helicase activity |
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