The role of adenosine triphosphate in the function of human origin recognition complex 4 protein

Human origin recognition complex 4 (ORC4) protein, a subunit of the origin recognition complex, belongs to the AAA+ superfamily of adenosine triphosphate (ATP) ases. Proteins belonging to this family require ATP for their function and interactions with ATP lead to conformational changes in them or i...

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Main Authors: ALEKSANDRA DIVAC, BRANKO TOMIĆ, JELENA KUŠIĆ
Format: Article
Language:English
Published: Serbian Chemical Society 2010-03-01
Series:Journal of the Serbian Chemical Society
Subjects:
Online Access:http://www.shd.org.rs/JSCS/Vol75/No3/03_4505_3963.pdf
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spelling doaj-3fc8702c481947baaa008a1be6fa97c72020-11-24T22:39:55ZengSerbian Chemical Society Journal of the Serbian Chemical Society0352-51392010-03-01753317322The role of adenosine triphosphate in the function of human origin recognition complex 4 proteinALEKSANDRA DIVACBRANKO TOMIĆJELENA KUŠIĆHuman origin recognition complex 4 (ORC4) protein, a subunit of the origin recognition complex, belongs to the AAA+ superfamily of adenosine triphosphate (ATP) ases. Proteins belonging to this family require ATP for their function and interactions with ATP lead to conformational changes in them or in their partners. Human ORC4 protein induces structural changes in DNA substrates, promoting renaturation and formation of non-canonical structures, as well as conversion of single-stranded into multi-stranded oligonucleotide structures. The aim of this study was to further investigate the role of ATP in the function of human ORC4 protein. For this purpose, a mutant in the conserved Walker B motif of ORC4, which is able to bind but not to hydrolyze ATP, was constructed and its activity in DNA restructuring reactions was investigated. The obtained results showed that ATP hydrolysis is not necessary for the function of human ORC4. It is proposed that ATP has a structural role as a cofactor in the function of human ORC4 as a DNA restructuring agent.http://www.shd.org.rs/JSCS/Vol75/No3/03_4505_3963.pdforigin recognition complex (ORC)adenosine triphosphate (ATP)DNA structureorigin selection
collection DOAJ
language English
format Article
sources DOAJ
author ALEKSANDRA DIVAC
BRANKO TOMIĆ
JELENA KUŠIĆ
spellingShingle ALEKSANDRA DIVAC
BRANKO TOMIĆ
JELENA KUŠIĆ
The role of adenosine triphosphate in the function of human origin recognition complex 4 protein
Journal of the Serbian Chemical Society
origin recognition complex (ORC)
adenosine triphosphate (ATP)
DNA structure
origin selection
author_facet ALEKSANDRA DIVAC
BRANKO TOMIĆ
JELENA KUŠIĆ
author_sort ALEKSANDRA DIVAC
title The role of adenosine triphosphate in the function of human origin recognition complex 4 protein
title_short The role of adenosine triphosphate in the function of human origin recognition complex 4 protein
title_full The role of adenosine triphosphate in the function of human origin recognition complex 4 protein
title_fullStr The role of adenosine triphosphate in the function of human origin recognition complex 4 protein
title_full_unstemmed The role of adenosine triphosphate in the function of human origin recognition complex 4 protein
title_sort role of adenosine triphosphate in the function of human origin recognition complex 4 protein
publisher Serbian Chemical Society
series Journal of the Serbian Chemical Society
issn 0352-5139
publishDate 2010-03-01
description Human origin recognition complex 4 (ORC4) protein, a subunit of the origin recognition complex, belongs to the AAA+ superfamily of adenosine triphosphate (ATP) ases. Proteins belonging to this family require ATP for their function and interactions with ATP lead to conformational changes in them or in their partners. Human ORC4 protein induces structural changes in DNA substrates, promoting renaturation and formation of non-canonical structures, as well as conversion of single-stranded into multi-stranded oligonucleotide structures. The aim of this study was to further investigate the role of ATP in the function of human ORC4 protein. For this purpose, a mutant in the conserved Walker B motif of ORC4, which is able to bind but not to hydrolyze ATP, was constructed and its activity in DNA restructuring reactions was investigated. The obtained results showed that ATP hydrolysis is not necessary for the function of human ORC4. It is proposed that ATP has a structural role as a cofactor in the function of human ORC4 as a DNA restructuring agent.
topic origin recognition complex (ORC)
adenosine triphosphate (ATP)
DNA structure
origin selection
url http://www.shd.org.rs/JSCS/Vol75/No3/03_4505_3963.pdf
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