title: The analysis of post-translational modifications of mouse H1 variants by MALDI mass spectrometry
metadata.name: dc.contributor.author
metadata.value: Starkova, Tatiana Yu.
metadata.lang: -
metadata.name: dc.contributor.author
metadata.value: Polyanichko, Alexander M.
metadata.lang: -
metadata.name: dc.contributor.author
metadata.value: Artamonova, Tatiana O.
metadata.lang: -
metadata.name: dc.contributor.author
metadata.value: Khodorkovskii, Mikhail A.
metadata.lang: -
metadata.name: dc.contributor.author
metadata.value: Chikhirzhina, Elena V.
metadata.lang: -
metadata.name: dc.contributor.author
metadata.value: Tomilin, Alexey N.
metadata.lang: -
metadata.name: dc.date.accessioned
metadata.value: 2017-03-20T15:31:30Z
metadata.lang: -
metadata.name: dc.date.available
metadata.value: 2017-03-20T15:31:30Z
metadata.lang: -
metadata.name: dc.date.issued
metadata.value: 2016-12
metadata.lang: -
metadata.name: dc.identifier.other
metadata.value: 10.21638/11701/spbu04.2016.407
metadata.lang: -
metadata.name: dc.identifier.uri
metadata.value: http://hdl.handle.net/11701/6108
metadata.lang: -
metadata.name: dc.description.abstract
metadata.value: The post-translational modifications of linker histone H1 variants from mouse thymus have been
  studied by MALDI mass spectrometry (matrix-assisted laser desorption/ionization). We have
  identified six subtypes of histone H1, extracted from the mouse thymus, such as H1.0, H1.1, H1.2,
  H1.3, H1.4 and H1.5. We have shown that the H1.1 variant is dominant. Analysis of the MS
  results led us to the conclusion that the types and positions of the posttranslational modifications
  in H1.2–H1.4 variants within the globular domain are highly conserved. The majority of the
  identified methylation and acetylation sites of the linker histone H1 subtypes occur in the globular
  domains of the proteins, e. g. K34, K52, K64, K85 and K97. We have revealed for the first time methylation site of lysine at position 34 in H1.4 (meK34–mH1.4) and H1.1 (meK34–mH1.4)
  variants. Refs 39. Figs 1. Tables 2.
metadata.lang: en_GB
metadata.name: dc.description.sponsorship
metadata.value: Работа выполнена при финансовой поддержке Российского фонда фундаментальных исследований
  (16-34-60174, 15-04-06993).
metadata.lang: en_GB
metadata.name: dc.language.iso
metadata.value: ru
metadata.lang: en_GB
metadata.name: dc.publisher
metadata.value: St Petersburg State University
metadata.lang: en_GB
metadata.name: dc.relation.ispartofseries
metadata.value: Vestnik of St Petersburg University. Series 4. Physics. Chemistry;Vol. 3 (61); Issue 4
metadata.lang: -
metadata.name: dc.subject
metadata.value: linker histone H1
metadata.lang: en_GB
metadata.name: dc.subject
metadata.value: post-translational modifications
metadata.lang: en_GB
metadata.name: dc.subject
metadata.value: 2D electrophoresis
metadata.lang: en_GB
metadata.name: dc.subject
metadata.value: MALDI mass spectrometry
metadata.lang: en_GB
metadata.name: dc.title
metadata.value: The analysis of post-translational modifications of mouse H1 variants by MALDI mass spectrometry
metadata.lang: en_GB
metadata.name: dc.type
metadata.value: Article
metadata.lang: en_GB
resources.filename: 07-Starkova.pdf
resources.url: https://dspace.spbu.ru/bitstream/11701/6108/1/07-Starkova.pdf
resources.format: Adobe PDF
resources.size: 363,43 kB