Cargando…
A Hypomorphic Mutant of PHD Domain Protein Male Meiocytes Death 1
Meiosis drives reciprocal genetic exchanges and produces gametes with halved chromosome number, which is important for the genetic diversity, plant viability, and ploidy consistency of flowering plants. Alterations in chromosome dynamics and/or cytokinesis during meiosis may lead to meiotic restitut...
Autores principales: | , , , , , , |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2021
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8066392/ https://www.ncbi.nlm.nih.gov/pubmed/33916197 http://dx.doi.org/10.3390/genes12040516 |
_version_ | 1783682562745434112 |
---|---|
author | Liu, Bing Jin, Chunlian De Storme, Nico Schotte, Sébastien Schindfessel, Cédric De Meyer, Tim Geelen, Danny |
author_facet | Liu, Bing Jin, Chunlian De Storme, Nico Schotte, Sébastien Schindfessel, Cédric De Meyer, Tim Geelen, Danny |
author_sort | Liu, Bing |
collection | PubMed |
description | Meiosis drives reciprocal genetic exchanges and produces gametes with halved chromosome number, which is important for the genetic diversity, plant viability, and ploidy consistency of flowering plants. Alterations in chromosome dynamics and/or cytokinesis during meiosis may lead to meiotic restitution and the formation of unreduced microspores. In this study, we isolated an Arabidopsis mutant male meiotic restitution 1 (mmr1), which produces a small subpopulation of diploid or polyploid pollen grains. Cytological analysis revealed that mmr1 produces dyads, triads, and monads indicative of male meiotic restitution. Both homologous chromosomes and sister chromatids in mmr1 are separated normally, but chromosome condensation at metaphase I is slightly affected. The mmr1 mutant displayed incomplete meiotic cytokinesis. Supportively, immunostaining of the microtubular cytoskeleton showed that the spindle organization at anaphase II and mini-phragmoplast formation at telophase II are aberrant. The causative mutation in mmr1 was mapped to chromosome 1 at the chromatin regulator Male Meiocyte Death 1 (MMD1/DUET) locus. mmr1 contains a C-to-T transition at the third exon of MMD1/DUET at the genomic position 2168 bp from the start codon, which causes an amino acid change G618D that locates in the conserved PHD-finger domain of histone binding proteins. The F1 progenies of mmr1 crossing with knockout mmd1/duet mutant exhibited same meiotic defects and similar meiotic restitution rate as mmr1. Taken together, we here report a hypomorphic mmd1/duet allele that typically shows defects in microtubule organization and cytokinesis. |
format | Online Article Text |
id | pubmed-8066392 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-80663922021-04-25 A Hypomorphic Mutant of PHD Domain Protein Male Meiocytes Death 1 Liu, Bing Jin, Chunlian De Storme, Nico Schotte, Sébastien Schindfessel, Cédric De Meyer, Tim Geelen, Danny Genes (Basel) Article Meiosis drives reciprocal genetic exchanges and produces gametes with halved chromosome number, which is important for the genetic diversity, plant viability, and ploidy consistency of flowering plants. Alterations in chromosome dynamics and/or cytokinesis during meiosis may lead to meiotic restitution and the formation of unreduced microspores. In this study, we isolated an Arabidopsis mutant male meiotic restitution 1 (mmr1), which produces a small subpopulation of diploid or polyploid pollen grains. Cytological analysis revealed that mmr1 produces dyads, triads, and monads indicative of male meiotic restitution. Both homologous chromosomes and sister chromatids in mmr1 are separated normally, but chromosome condensation at metaphase I is slightly affected. The mmr1 mutant displayed incomplete meiotic cytokinesis. Supportively, immunostaining of the microtubular cytoskeleton showed that the spindle organization at anaphase II and mini-phragmoplast formation at telophase II are aberrant. The causative mutation in mmr1 was mapped to chromosome 1 at the chromatin regulator Male Meiocyte Death 1 (MMD1/DUET) locus. mmr1 contains a C-to-T transition at the third exon of MMD1/DUET at the genomic position 2168 bp from the start codon, which causes an amino acid change G618D that locates in the conserved PHD-finger domain of histone binding proteins. The F1 progenies of mmr1 crossing with knockout mmd1/duet mutant exhibited same meiotic defects and similar meiotic restitution rate as mmr1. Taken together, we here report a hypomorphic mmd1/duet allele that typically shows defects in microtubule organization and cytokinesis. MDPI 2021-04-01 /pmc/articles/PMC8066392/ /pubmed/33916197 http://dx.doi.org/10.3390/genes12040516 Text en © 2021 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Article Liu, Bing Jin, Chunlian De Storme, Nico Schotte, Sébastien Schindfessel, Cédric De Meyer, Tim Geelen, Danny A Hypomorphic Mutant of PHD Domain Protein Male Meiocytes Death 1 |
title | A Hypomorphic Mutant of PHD Domain Protein Male Meiocytes Death 1 |
title_full | A Hypomorphic Mutant of PHD Domain Protein Male Meiocytes Death 1 |
title_fullStr | A Hypomorphic Mutant of PHD Domain Protein Male Meiocytes Death 1 |
title_full_unstemmed | A Hypomorphic Mutant of PHD Domain Protein Male Meiocytes Death 1 |
title_short | A Hypomorphic Mutant of PHD Domain Protein Male Meiocytes Death 1 |
title_sort | hypomorphic mutant of phd domain protein male meiocytes death 1 |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8066392/ https://www.ncbi.nlm.nih.gov/pubmed/33916197 http://dx.doi.org/10.3390/genes12040516 |
work_keys_str_mv | AT liubing ahypomorphicmutantofphddomainproteinmalemeiocytesdeath1 AT jinchunlian ahypomorphicmutantofphddomainproteinmalemeiocytesdeath1 AT destormenico ahypomorphicmutantofphddomainproteinmalemeiocytesdeath1 AT schottesebastien ahypomorphicmutantofphddomainproteinmalemeiocytesdeath1 AT schindfesselcedric ahypomorphicmutantofphddomainproteinmalemeiocytesdeath1 AT demeyertim ahypomorphicmutantofphddomainproteinmalemeiocytesdeath1 AT geelendanny ahypomorphicmutantofphddomainproteinmalemeiocytesdeath1 AT liubing hypomorphicmutantofphddomainproteinmalemeiocytesdeath1 AT jinchunlian hypomorphicmutantofphddomainproteinmalemeiocytesdeath1 AT destormenico hypomorphicmutantofphddomainproteinmalemeiocytesdeath1 AT schottesebastien hypomorphicmutantofphddomainproteinmalemeiocytesdeath1 AT schindfesselcedric hypomorphicmutantofphddomainproteinmalemeiocytesdeath1 AT demeyertim hypomorphicmutantofphddomainproteinmalemeiocytesdeath1 AT geelendanny hypomorphicmutantofphddomainproteinmalemeiocytesdeath1 |