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Functional dissection of Drosophila melanogaster SUUR protein influence on H3K27me3 profile. / Posukh, Olga V.; Maksimov, Daniil A.; Laktionov, Petr P. et al.
In: Epigenetics and Chromatin, Vol. 10, No. 1, 56, 01.12.2017, p. 56.Research output: Contribution to journal › Article › peer-review
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TY - JOUR
T1 - Functional dissection of Drosophila melanogaster SUUR protein influence on H3K27me3 profile
AU - Posukh, Olga V.
AU - Maksimov, Daniil A.
AU - Laktionov, Petr P.
AU - Koryakov, Dmitry E.
AU - Belyakin, Stepan N.
PY - 2017/12/1
Y1 - 2017/12/1
N2 - Background: In eukaryotes, heterochromatin replicates late in S phase of the cell cycle and contains specific covalent modifications of histones. SuUR mutation found in Drosophila makes heterochromatin replicate earlier than in wild type and reduces the level of repressive histone modifications. SUUR protein was shown to be associated with moving replication forks, apparently through the interaction with PCNA. The biological process underlying the effects of SUUR on replication and composition of heterochromatin remains unknown. Results: Here we performed a functional dissection of SUUR protein effects on H3K27me3 level. Using hidden Markow model-based algorithm we revealed SuUR-sensitive chromosomal regions that demonstrated unusual characteristics: They do not contain Polycomb and require SUUR function to sustain H3K27me3 level. We tested the role of SUUR protein in the mechanisms that could affect H3K27me3 histone levels in these regions. We found that SUUR does not affect the initial H3K27me3 pattern formation in embryogenesis or Polycomb distribution in the chromosomes. We also ruled out the possible effect of SUUR on histone genes expression and its involvement in DSB repair. Conclusions: Obtained results support the idea that SUUR protein contributes to the heterochromatin maintenance during the chromosome replication. A model that explains major SUUR-associated phenotypes is proposed.
AB - Background: In eukaryotes, heterochromatin replicates late in S phase of the cell cycle and contains specific covalent modifications of histones. SuUR mutation found in Drosophila makes heterochromatin replicate earlier than in wild type and reduces the level of repressive histone modifications. SUUR protein was shown to be associated with moving replication forks, apparently through the interaction with PCNA. The biological process underlying the effects of SUUR on replication and composition of heterochromatin remains unknown. Results: Here we performed a functional dissection of SUUR protein effects on H3K27me3 level. Using hidden Markow model-based algorithm we revealed SuUR-sensitive chromosomal regions that demonstrated unusual characteristics: They do not contain Polycomb and require SUUR function to sustain H3K27me3 level. We tested the role of SUUR protein in the mechanisms that could affect H3K27me3 histone levels in these regions. We found that SUUR does not affect the initial H3K27me3 pattern formation in embryogenesis or Polycomb distribution in the chromosomes. We also ruled out the possible effect of SUUR on histone genes expression and its involvement in DSB repair. Conclusions: Obtained results support the idea that SUUR protein contributes to the heterochromatin maintenance during the chromosome replication. A model that explains major SUUR-associated phenotypes is proposed.
KW - Drosophila
KW - Epigenetic inheritance
KW - H3K27me3
KW - Heterochromatin
KW - Polycomb
KW - Replication
KW - Heterochromatin/metabolism
KW - Polycomb-Group Proteins/metabolism
KW - Drosophila Proteins/genetics
KW - Drosophila melanogaster/metabolism
KW - Algorithms
KW - Animals
KW - Histones/genetics
KW - Mutation
KW - POLYTENE CHROMOSOMES
KW - CHROMATIN
KW - HP1
KW - DNA UNDERREPLICATION
KW - GENOME
KW - REPLICATION
KW - GENE
KW - HISTONE H3
KW - CELL-CYCLE
KW - INTERCALARY HETEROCHROMATIN
UR - http://www.scopus.com/inward/record.url?scp=85037028913&partnerID=8YFLogxK
U2 - 10.1186/s13072-017-0163-z
DO - 10.1186/s13072-017-0163-z
M3 - Article
C2 - 29191233
AN - SCOPUS:85037028913
VL - 10
SP - 56
JO - Epigenetics and Chromatin
JF - Epigenetics and Chromatin
SN - 1756-8935
IS - 1
M1 - 56
ER -
ID: 10501188