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Identification of novel post-translational modifications in linke | 29233
Journal of Proteomics & Bioinformatics

Journal of Proteomics & Bioinformatics
Open Access

ISSN: 0974-276X

+44 1223 790975

Identification of novel post-translational modifications in linker histones from chicken erythrocytes


5th International Conference on Proteomics & Bioinformatics

September 01-03, 2015 Valencia, Spain

Alicia Roque

Universitat Aut�?²noma de Barcelona, Spain

Posters-Accepted Abstracts: J Proteomics Bioinform

Abstract :

Chicken erythrocyte nuclei were digested with micrococcal nuclease and fractionated by centrifugation in low-salt buffer into soluble and insoluble fractions. Post-translational modifications of the purified linker histones of both fractions were analyzed by LC-ESI-MS/MS. All six histone H1 subtypes (H1.01, H1.02, H1.03, H1.10, H1.1L and H1.1R) and histone H5 were identified. Mass spectrometry analysis enabled the identification of a wide range of PTMs including N�?±-terminal acetylation, acetylation, formylation, phosphorylation and oxidation. A total of nine new modifications in chicken linker histones were mapped, most of them located in the N-terminal and globular domains. Relative quantification of the modified peptides showed that linker histone PTMs were differentially distributed among both chromatin fractions suggesting their relevance in the regulation of chromatin structure. The analysis of our results combined with previously reported data for chicken and some mammalian species showed that most of the modified positions were conserved throughout evolution highlighting their importance in specific linker histone functions and epigenetics.

Biography :

Email: aroquec@yahoo.com

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