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- Kostova-Koleva, Nora N.Linköpings universitet,Institutionen för klinisk och experimentell medicin,Hälsouniversitetet (författare)
Histone H5chromatin interactions in situ are strongly modulated by H5 C-terminal phosphorylation
- Artikel/kapitelEngelska2013
Förlag, utgivningsår, omfång ...
- 2012-10-18
- Wiley-Blackwell,2013
- printrdacarrier
Nummerbeteckningar
- LIBRIS-ID:oai:DiVA.org:liu-90191
- https://urn.kb.se/resolve?urn=urn:nbn:se:liu:diva-90191URI
- https://doi.org/10.1002/cyto.a.22221DOI
Kompletterande språkuppgifter
- Språk:engelska
- Sammanfattning på:engelska
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- SwePubSwePub
Klassifikation
Anmärkningar
- Funding Agencies|Bulgarian National Science Fund|K-906/1999|Swedish Research Council|349-2001-6688|European Science Foundation EUROCORES Programme EuroDYNA (Austrian Science Foundation)|I23-B03|EC Sixth Framework Programme|ERAS-CT-2003-980409|
- We used linker histone-depleted normal human fibroblast nuclei as templates to study how phosphorylation affects histone H5 binding to chromatin in situ. Permeabilized cells were treated with 0.7 M NaCl to extract the native linker histones. Histone H5 was purified from chicken erythrocytes and phosphorylated in vitro by recombinant cdk5/p35 kinase. High performance capillary electrophoresis (HPCE) showed that the phosphorylated protein contained a mixture of multiply phosphorylated forms. Control experiments, using mass spectrometry, revealed that up to five SPXK motifs in the C terminus were phosphorylated, but also that about 10% of the protein contained one phosphoserine in the N-terminus. Reconstitution of H1-depleted fibroblast nuclei with nonphosphorylated or phosphorylated H5 was performed at physiological ionic strength. The bound H5 was then extracted using NaCl concentrations in the range of 0.15 to 0.7 M. The release of the H5 molecules was monitored by DAPI staining and image cytofluorometry. Our results show that H5 phosphorylation substantially reduced its affinity for chromatin in situ, which support previous observations indicating that C-terminal phosphorylation may be essential for the biological functions of linker histones.
Ämnesord och genrebeteckningar
- chromatin
- linker histones
- affinity
- phosphorylation
- MEDICINE
- MEDICIN
Biuppslag (personer, institutioner, konferenser, titlar ...)
- Srebreva, LjubaBulgarian Academic Science, Bulgaria (författare)
- Markov, Dimiter V.Bulgarian Academic Science, Bulgaria (författare)
- Sarg, BettinaMedical University of Innsbruck, Austria (författare)
- Lindner, Herbert H.Medical University of Innsbruck, Austria (författare)
- Rundquist, IngemarLinköpings universitet,Cellbiologi,Hälsouniversitetet(Swepub:liu)ingru73 (författare)
- Linköpings universitetInstitutionen för klinisk och experimentell medicin (creator_code:org_t)
Sammanhörande titlar
- Ingår i:Cytometry Part A: Wiley-Blackwell83A:3, s. 273-2791552-49221552-4930
Internetlänk
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- Kostova-Koleva, ...
- Srebreva, Ljuba
- Markov, Dimiter ...
- Sarg, Bettina
- Lindner, Herbert ...
- Rundquist, Ingem ...
- Artiklar i publikationen
- Cytometry Part A
- Av lärosätet
- Linköpings universitet
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