Phosphorylation of HORMA-domain protein HTP-3 at Serine 285 is
dispensable for crossover formation

J 2022

Phosphorylation of HORMA-domain protein HTP-3 at Serine 285 is dispensable for crossover formation

DAS, Debabrata; Shalini TRIVEDI; Jitka BLAŽÍČKOVÁ; Swathi ARUR; Nicola SILVA et. al.

Basic information

Original name

Phosphorylation of HORMA-domain protein HTP-3 at Serine 285 is dispensable for crossover formation

Authors

DAS, Debabrata; Shalini TRIVEDI (356 India, belonging to the institution); Jitka BLAŽÍČKOVÁ (203 Czech Republic, belonging to the institution); Swathi ARUR and Nicola SILVA (380 Italy, guarantor, belonging to the institution)

Edition

G3-Genes, Genomes, Genetics, CARY, OXFORD UNIV PRESS INC, 2022, 2160-1836

Other information

Language

English

Type of outcome

Article in a journal

Field of Study

10603 Genetics and heredity

Country of publisher

United States of America

Confidentiality degree

is not subject to a state or trade secret

References:

URL

Impact factor

Impact factor: 2.600

RIV identification code

RIV/00216224:14110/22:00128180

Organization unit

Faculty of Medicine

DOI

http://dx.doi.org/10.1093/g3journal/jkac079

UT WoS

000786255000001

EID Scopus

2-s2.0-85130188283

Keywords in English

Caenorhabditis elegans meiosis; HORMA-domain proteins; HTP-3

Abstract

V originále

Generation of functional gametes is accomplished through a multilayered and finely orchestrated succession of events during meiotic progression. In the Caenorhabditis elegans germline, the HORMA-domain-containing protein HTP-3 plays pivotal roles for the establishment of chromosome axes and the efficient induction of programmed DNA double-strand breaks, both of which are crucial for crossover formation. Double-strand breaks allow for accurate chromosome segregation during the first meiotic division and therefore are an essential requirement for the production of healthy gametes. Phosphorylation-dependent regulation of HORMAD protein plays important roles in controlling meiotic chromosome behavior. Here, we document a phospho-site in HTP-3 at Serine 285 that is constitutively phosphorylated during meiotic prophase I. pHTP-3(S285) localization overlaps with panHTP-3 except in nuclei undergoing physiological apoptosis, in which pHTP-3 is absent. Surprisingly, we observed that phosphorylation of HTP-3 at S285 is independent of the canonical kinases that control meiotic progression in nematodes. During meiosis, the htp-3(S285A) mutant displays accelerated RAD-51 turnover, but no other meiotic abnormalities. Altogether, these data indicate that the Ser285 phosphorylation is independent of canonical meiotic protein kinases and does not regulate HTP-3-dependent meiotic processes. We propose a model wherein phosphorylation of HTP-3 occurs through noncanonical or redundant meiotic kinases and/or is likely redundant with additional phospho-sites for function in vivo.

Links

GA20-08819S, research and development project

Name: Pochopení úlohy PARG při podpoře tvorby a oprav dvouřetězcových zlomů DNA v meióze

Investor: Czech Science Foundation

MUNI/A/1418/2021, interní kód MU

Name: Biomedicínské vědy II (Acronym: BIOMED)

Investor: Masaryk University

90129, large research infrastructures

Name: Czech-BioImaging II

Cite

DAS, Debabrata; Shalini TRIVEDI; Jitka BLAŽÍČKOVÁ; Swathi ARUR and Nicola SILVA. Phosphorylation of HORMA-domain protein HTP-3 at Serine 285 is dispensable for crossover formation. G3-Genes, Genomes, Genetics. CARY: OXFORD UNIV PRESS INC, 2022, vol. 12, No 5, p. 1-10. ISSN 2160-1836. Available from: https://dx.doi.org/10.1093/g3journal/jkac079.

@article{2248093,
   author = {Das, Debabrata and Trivedi, Shalini and Blažíčková, Jitka and Arur, Swathi and Silva, Nicola},
   article_location = {CARY},
   article_number = {5},
   doi = {http://dx.doi.org/10.1093/g3journal/jkac079},
   keywords = {Caenorhabditis elegans meiosis; HORMA-domain proteins; HTP-3},
   language = {eng},
   issn = {2160-1836},
   journal = {G3-Genes, Genomes, Genetics},
   title = {Phosphorylation of HORMA-domain protein HTP-3 at Serine 285 is dispensable for crossover formation},
   url = {https://academic.oup.com/g3journal/article/12/5/jkac079/6564663?login=true},
   volume = {12},
   year = {2022}
}

TY  - JOUR
ID  - 2248093
AU  - Das, Debabrata - Trivedi, Shalini - Blažíčková, Jitka - Arur, Swathi - Silva, Nicola
PY  - 2022
TI  - Phosphorylation of HORMA-domain protein HTP-3 at Serine 285 is dispensable for crossover formation
JF  - G3-Genes, Genomes, Genetics
VL  - 12
IS  - 5
SP  - 1-10
EP  - 1-10
PB  - OXFORD UNIV PRESS INC
SN  - 21601836
KW  - Caenorhabditis elegans meiosis
KW  - HORMA-domain proteins
KW  - HTP-3
UR  - https://academic.oup.com/g3journal/article/12/5/jkac079/6564663?login=true
N2  - Generation of functional gametes is accomplished through a multilayered and finely orchestrated succession of events during meiotic progression. In the Caenorhabditis elegans germline, the HORMA-domain-containing protein HTP-3 plays pivotal roles for the establishment of chromosome axes and the efficient induction of programmed DNA double-strand breaks, both of which are crucial for crossover formation. Double-strand breaks allow for accurate chromosome segregation during the first meiotic division and therefore are an essential requirement for the production of healthy gametes. Phosphorylation-dependent regulation of HORMAD protein plays important roles in controlling meiotic chromosome behavior. Here, we document a phospho-site in HTP-3 at Serine 285 that is constitutively phosphorylated during meiotic prophase I. pHTP-3(S285) localization overlaps with panHTP-3 except in nuclei undergoing physiological apoptosis, in which pHTP-3 is absent. Surprisingly, we observed that phosphorylation of HTP-3 at S285 is independent of the canonical kinases that control meiotic progression in nematodes. During meiosis, the htp-3(S285A) mutant displays accelerated RAD-51 turnover, but no other meiotic abnormalities. Altogether, these data indicate that the Ser285 phosphorylation is independent of canonical meiotic protein kinases and does not regulate HTP-3-dependent meiotic processes. We propose a model wherein phosphorylation of HTP-3 occurs through noncanonical or redundant meiotic kinases and/or is likely redundant with additional phospho-sites for function in vivo.
ER  -

DAS, Debabrata; Shalini TRIVEDI; Jitka BLAŽÍČKOVÁ; Swathi ARUR and Nicola SILVA. Phosphorylation of HORMA-domain protein HTP-3 at Serine 285 is dispensable for crossover formation. \textit{G3-Genes, Genomes, Genetics}. CARY: OXFORD UNIV PRESS INC, 2022, vol.~12, No~5, p.~1-10. ISSN~2160-1836. Available from: https://dx.doi.org/10.1093/g3journal/jkac079.

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