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Production and characterization of recombinant protein preparations of Endonuclease G-homologs from yeast, C. elegans and humans

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dc.contributor.author Kieper J.
dc.contributor.author Lauber C.
dc.contributor.author Gimadutdinow O.
dc.contributor.author Urbaǹska A.
dc.contributor.author Cymerman I.
dc.contributor.author Ghosh M.
dc.contributor.author Szczesny B.
dc.contributor.author Meiss G.
dc.date.accessioned 2018-09-18T20:13:56Z
dc.date.available 2018-09-18T20:13:56Z
dc.date.issued 2010
dc.identifier.issn 1046-5928
dc.identifier.uri https://dspace.kpfu.ru/xmlui/handle/net/137786
dc.description.abstract Nuc1p, CPS-6, EndoG and EXOG are evolutionary conserved mitochondrial nucleases from yeast, Caenorhabditis elegans and humans, respectively. These enzymes play an important role in programmed cell death as well as mitochondrial DNA-repair and recombination. Whereas a significant interest has been given to the cell biology of these proteins, in particular their recruitment during caspase-independent apoptosis, determination of their biochemical properties has lagged behind. In part, biochemical as well as structural analysis of mitochondrial nucleases has been hampered by the fact that upon cloning and overexpression in Escherichia coli these enzymes can exert considerable toxicity and tend to aggregate and form inclusion bodies. We have, therefore, established a uniform E. coli expression system allowing us to obtain these four evolutionary related nucleases in active form from the soluble as well as insoluble fractions of E. coli cell lysates. Using preparations of recombinant Nuc1p, CPS-6, EndoG and EXOG we have compared biochemical properties and the substrate specificities of these related nucleases on selected substrates in parallel. Whereas Nuc1p and EXOG in addition to their endonuclease activity exert 5'-3'- exonuclease activity, CPS-6 and EndoG predominantly are endonucleases. These findings allow speculating that the mechanisms of action of these related nucleases in cell death as well as DNA-repair and recombination differ according to their enzyme activities and substrate specificities. © 2010 Elsevier Inc. All rights reserved.
dc.relation.ispartofseries Protein Expression and Purification
dc.subject Apoptosis
dc.subject DNA-repair
dc.subject Endonuclease
dc.subject Exonuclease
dc.subject Mitochondria
dc.subject Refolding
dc.title Production and characterization of recombinant protein preparations of Endonuclease G-homologs from yeast, C. elegans and humans
dc.type Article
dc.relation.ispartofseries-issue 1
dc.relation.ispartofseries-volume 73
dc.collection Публикации сотрудников КФУ
dc.relation.startpage 99
dc.source.id SCOPUS10465928-2010-73-1-SID77955365267

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  • Публикации сотрудников КФУ Scopus [24551]
    Коллекция содержит публикации сотрудников Казанского федерального (до 2010 года Казанского государственного) университета, проиндексированные в БД Scopus, начиная с 1970г.

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