A motor independent requirement for dynein light chain in Caenorhabditis elegans meiotic synapsis
Abstract The dynein motor complex is thought to aid in homolog pairing in many organisms by moving chromosomes within the nuclear periphery to promote and test homologous interactions. This precedes synaptonemal complex (SC) formation during homolog synapsis, which stabilizes homolog proximity durin...
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Published in | Genetics (Austin) Vol. 220; no. 1 |
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Main Authors | , , , , |
Format | Journal Article |
Language | English |
Published |
United States
Oxford University Press
04.01.2022
Genetics Society of America |
Subjects | |
Online Access | Get full text |
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Summary: | Abstract
The dynein motor complex is thought to aid in homolog pairing in many organisms by moving chromosomes within the nuclear periphery to promote and test homologous interactions. This precedes synaptonemal complex (SC) formation during homolog synapsis, which stabilizes homolog proximity during recombination. We observed that depletion of the dynein light chain (DLC-1) in Caenorhabditis elegans irreversibly prevents synapsis, causing an increase in off-chromatin formation of SC protein foci with increasing temperature. This requirement for DLC-1 is independent of its function in dynein motors, as SYP protein foci do not form with depletion of other dynein motor components. In contrast to normal SC-related structures, foci formed with DLC-1 depletion are resistant to dissolution with 1,6-hexanediol, similar to aggregates of SC proteins formed in high growth temperatures. Dynein light chains have been shown to act as hub proteins that interact with other proteins through a conserved binding motif. We identified a similar DLC-1 binding motif in the C. elegans SC protein SYP-2, and mutation of the putative motif causes meiosis defects that are exacerbated by elevated temperatures. We propose that DLC-1 acts as a pre-synapsis chaperone-like factor for SYP proteins to help regulate their self-association prior to the signals for SC assembly, a role that is revealed by its increased essentiality at elevated temperatures. |
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Bibliography: | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 Present address: Department of Pediatrics, Washington University in St. Louis School of Medicine, Saint Louis, MI 63110, USA. Present address: C. elegans Model Organism Screening Center, Washington University in St. Louis School of Medicine, Saint Louis, MI 63110, USA. |
ISSN: | 1943-2631 0016-6731 1943-2631 |
DOI: | 10.1093/genetics/iyab203 |