| Форма представления | Статьи в зарубежных журналах и сборниках |
| Год публикации | 2017 |
| Язык | английский |
|
Хайруллин Рафиль Фидаилевич, автор
|
|
Wanrooij Sjoerd , автор
|
| Библиографическое описание на языке оригинала |
Boldinova EO, Stojkovič G, Khairullin R,
Wanrooij S, Makarova AV (2017) Optimization of
the expression, purification and polymerase activity
reaction conditions of recombinant human
PrimPol. PLoS ONE 12(9): e0184489. https://doi.
org/10.1371/journal.pone.0184489 |
| Аннотация |
Human PrimPol is a DNA primase/polymerase involved in DNA damage tolerance and prevents nuclear genome instability. PrimPol is also localized to the mitochondria, but its precise function in mitochondrial DNA maintenance has remained elusive. PrimPol works both as a translesion (TLS) polymerase and as the primase that restarts DNA replication after a lesion. However, the observed biochemical activities of PrimPol vary considerably between studies as a result of different reaction conditions used. To reveal the effects of reaction composition on PrimPol DNA polymerase activity, we tested the polymerase activity in the presence of various buffer agents, salt concentrations, pH values and metal cofactors. Additionally, the enzyme stability was analyzed under various conditions. We demonstrate that the reaction buffer with pH 6–6.5, low salt concentrations and 3 mM Mg²⁺ or 0.3–3 mM Mn²⁺ cofactor ions supports the highest DNA polymerase activity of human PrimPol in vitro. The DNA polymerase |
| Ключевые слова |
PrimPol, DNA polymerase, mitochondria, protein expression. |
| Название журнала |
PLos ONE
|
| URL |
http://journals.plos.org/plosone/article?id=10.1371/journal.pone.0184489 |
| Пожалуйста, используйте этот идентификатор, чтобы цитировать или ссылаться на эту карточку |
https://repository.kpfu.ru/?p_id=163498 |
| Файлы ресурса | |
|
|
Полная запись метаданных  |
| Поле DC |
Значение |
Язык |
| dc.contributor.author |
Хайруллин Рафиль Фидаилевич |
ru_RU |
| dc.contributor.author |
Wanrooij Sjoerd |
ru_RU |
| dc.date.accessioned |
2017-01-01T00:00:00Z |
ru_RU |
| dc.date.available |
2017-01-01T00:00:00Z |
ru_RU |
| dc.date.issued |
2017 |
ru_RU |
| dc.identifier.citation |
Boldinova EO, Stojkovič G, Khairullin R,
Wanrooij S, Makarova AV (2017) Optimization of
the expression, purification and polymerase activity
reaction conditions of recombinant human
PrimPol. PLoS ONE 12(9): e0184489. https://doi.
org/10.1371/journal.pone.0184489 |
ru_RU |
| dc.identifier.uri |
https://repository.kpfu.ru/?p_id=163498 |
ru_RU |
| dc.description.abstract |
PLos ONE |
ru_RU |
| dc.description.abstract |
Human PrimPol is a DNA primase/polymerase involved in DNA damage tolerance and prevents nuclear genome instability. PrimPol is also localized to the mitochondria, but its precise function in mitochondrial DNA maintenance has remained elusive. PrimPol works both as a translesion (TLS) polymerase and as the primase that restarts DNA replication after a lesion. However, the observed biochemical activities of PrimPol vary considerably between studies as a result of different reaction conditions used. To reveal the effects of reaction composition on PrimPol DNA polymerase activity, we tested the polymerase activity in the presence of various buffer agents, salt concentrations, pH values and metal cofactors. Additionally, the enzyme stability was analyzed under various conditions. We demonstrate that the reaction buffer with pH 6–6.5, low salt concentrations and 3 mM Mg²⁺ or 0.3–3 mM Mn²⁺ cofactor ions supports the highest DNA polymerase activity of human PrimPol in vitro. The DNA polymerase |
ru_RU |
| dc.language.iso |
ru |
ru_RU |
| dc.subject |
PrimPol |
ru_RU |
| dc.subject |
DNA polymerase |
ru_RU |
| dc.subject |
mitochondria |
ru_RU |
| dc.subject |
protein expression. |
ru_RU |
| dc.title |
Optimization of the expression, purification and polymerase activity reaction conditions of recombinant human PrimPol |
ru_RU |
| dc.type |
Статьи в зарубежных журналах и сборниках |
ru_RU |
|
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