Post-translational modifications of linker histone H1 variants in mammals

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Post-translational modifications of linker histone H1 variants in mammals. / Starkova, T. Yu; Polyanichko, A. M.; Artamonova, T. O.; Khodorkovskii, M. A.; Kostyleva, E. I.; Chikhirzhina, E. V.; Tomilin, A. N.

In: Physical Biology, Vol. 14, No. 1, 016005, 16.02.2017.

Research output: Contribution to journal › Article › peer-review

Author

Starkova, T. Yu ; Polyanichko, A. M. ; Artamonova, T. O. ; Khodorkovskii, M. A. ; Kostyleva, E. I. ; Chikhirzhina, E. V. ; Tomilin, A. N. / Post-translational modifications of linker histone H1 variants in mammals. In: Physical Biology. 2017 ; Vol. 14, No. 1.

BibTeX

@article{a95fc2a5177946daa6163b1036ff60d6,

title = "Post-translational modifications of linker histone H1 variants in mammals",

abstract = "The covalent modifications of the linker histone H1 and the core histones are thought to play an important role in the control of chromatin functioning. Histone H1 variants from K562 cell line (hH1), mouse (mH1) and calf (cH1) thymi were studied by matrix-activated laser desorption/ionization fourier transform ion cyclotron resonance mass-spectroscopy (MALDI-FT-ICR-MS). The proteomics analysis revealed novel post-translational modifications of the histone H1, such as meK34-mH1.4, meK35-cH1.1, meK35-mH1.1, meK75-hH1.2, meK75-hH1.3, acK26-hH1.4, acK26-hH1.3 and acK17-hH1.1. The comparison of the hH1, mH1 and cH1 proteins has demonstrated that the types and positions of the post-translational modifications of the globular domains of the H1.2-H1.4 variants are very conservative. However, the post-translational modifications of the N- and C-terminal tails of H1.2, H1.3 and H1.4 are different. The differences of post-translational modifications in the N- and C-terminal tails of H1.2, H1.3 and H1.4 likely lead to the differences in DNA-H1 and H1-protein interactions.",

keywords = "2D electrophoresis, linker histone H1, MALDI mass spectrometry, post-translational modifications",

author = "Starkova, {T. Yu} and Polyanichko, {A. M.} and Artamonova, {T. O.} and Khodorkovskii, {M. A.} and Kostyleva, {E. I.} and Chikhirzhina, {E. V.} and Tomilin, {A. N.}",

year = "2017",

month = feb,

day = "16",

doi = "10.1088/1478-3975/aa551a",

language = "English",

volume = "14",

journal = "Physical Biology",

issn = "1478-3967",

publisher = "IOP Publishing Ltd.",

number = "1",

}

RIS

TY - JOUR

T1 - Post-translational modifications of linker histone H1 variants in mammals

AU - Starkova, T. Yu

AU - Polyanichko, A. M.

AU - Artamonova, T. O.

AU - Khodorkovskii, M. A.

AU - Kostyleva, E. I.

AU - Chikhirzhina, E. V.

AU - Tomilin, A. N.

PY - 2017/2/16

Y1 - 2017/2/16

N2 - The covalent modifications of the linker histone H1 and the core histones are thought to play an important role in the control of chromatin functioning. Histone H1 variants from K562 cell line (hH1), mouse (mH1) and calf (cH1) thymi were studied by matrix-activated laser desorption/ionization fourier transform ion cyclotron resonance mass-spectroscopy (MALDI-FT-ICR-MS). The proteomics analysis revealed novel post-translational modifications of the histone H1, such as meK34-mH1.4, meK35-cH1.1, meK35-mH1.1, meK75-hH1.2, meK75-hH1.3, acK26-hH1.4, acK26-hH1.3 and acK17-hH1.1. The comparison of the hH1, mH1 and cH1 proteins has demonstrated that the types and positions of the post-translational modifications of the globular domains of the H1.2-H1.4 variants are very conservative. However, the post-translational modifications of the N- and C-terminal tails of H1.2, H1.3 and H1.4 are different. The differences of post-translational modifications in the N- and C-terminal tails of H1.2, H1.3 and H1.4 likely lead to the differences in DNA-H1 and H1-protein interactions.

AB - The covalent modifications of the linker histone H1 and the core histones are thought to play an important role in the control of chromatin functioning. Histone H1 variants from K562 cell line (hH1), mouse (mH1) and calf (cH1) thymi were studied by matrix-activated laser desorption/ionization fourier transform ion cyclotron resonance mass-spectroscopy (MALDI-FT-ICR-MS). The proteomics analysis revealed novel post-translational modifications of the histone H1, such as meK34-mH1.4, meK35-cH1.1, meK35-mH1.1, meK75-hH1.2, meK75-hH1.3, acK26-hH1.4, acK26-hH1.3 and acK17-hH1.1. The comparison of the hH1, mH1 and cH1 proteins has demonstrated that the types and positions of the post-translational modifications of the globular domains of the H1.2-H1.4 variants are very conservative. However, the post-translational modifications of the N- and C-terminal tails of H1.2, H1.3 and H1.4 are different. The differences of post-translational modifications in the N- and C-terminal tails of H1.2, H1.3 and H1.4 likely lead to the differences in DNA-H1 and H1-protein interactions.

KW - 2D electrophoresis

KW - linker histone H1

KW - MALDI mass spectrometry

KW - post-translational modifications

UR - http://www.scopus.com/inward/record.url?scp=85016276462&partnerID=8YFLogxK

U2 - 10.1088/1478-3975/aa551a

DO - 10.1088/1478-3975/aa551a

M3 - Article

C2 - 28000612

VL - 14

JO - Physical Biology

JF - Physical Biology

SN - 1478-3967

IS - 1

M1 - 016005

ER -

ID: 7733153