scholarly journals Regulating chromosomal movement by the cochaperone FKB-6 ensures timely pairing and synapsis

2017 ◽  
Vol 216 (2) ◽  
pp. 393-408 ◽  
Author(s):  
Benjamin Alleva ◽  
Nathan Balukoff ◽  
Amy Peiper ◽  
Sarit Smolikove
Keyword(s):  
Nuclear Envelope ◽  
Chromosome Pairing ◽  
Meiotic Prophase ◽  
Homologous Chromosome ◽  
Strand Break ◽  
Crossing Over ◽  
Chromosome Movement ◽  
Microtubule Network ◽  
Homologous Chromosome Pairing ◽  
Proper Movement

In meiotic prophase I, homologous chromosome pairing is promoted through chromosome movement mediated by nuclear envelope proteins, microtubules, and dynein. After proper homologue pairing has been established, the synaptonemal complex (SC) assembles along the paired homologues, stabilizing their interaction and allowing for crossing over to occur. Previous studies have shown that perturbing chromosome movement leads to pairing defects and SC polycomplex formation. We show that FKB-6 plays a role in SC assembly and is required for timely pairing and proper double-strand break repair kinetics. FKB-6 localizes outside the nucleus, and in its absence, the microtubule network is altered. FKB-6 is required for proper movement of dynein, increasing resting time between movements. Attenuating chromosomal movement in fkb-6 mutants partially restores the defects in synapsis, in agreement with FKB-6 acting by decreasing chromosomal movement. Therefore, we suggest that FKB-6 plays a role in regulating dynein movement by preventing excess chromosome movement, which is essential for proper SC assembly and homologous chromosome pairing.

scholarly journals Bypass of a Meiotic Checkpoint by Overproduction of Meiotic Chromosomal Proteins

2000 ◽  
Vol 20 (13) ◽  
pp. 4838-4848 ◽  
Author(s):  
Julie M. Bailis ◽  
Albert V. Smith ◽  
G. Shirleen Roeder
Keyword(s):  
Meiotic Recombination ◽  
Meiotic Prophase ◽  
Homologous Chromosome ◽  
Strand Break ◽  
Chromosomal Protein ◽  
Chromosomal Proteins ◽  
Cycle Arrest ◽  
Homologous Chromosome Pairing ◽  
Synaptonemal Complex Formation ◽  
Break Formation

ABSTRACT The Saccharomyces cerevisiae zip1 mutant, which exhibits defects in synaptonemal complex formation and meiotic recombination, triggers a checkpoint that causes cells to arrest at the pachytene stage of meiotic prophase. Overproduction of either the meiotic chromosomal protein Red1 or the meiotic kinase Mek1 bypasses this checkpoint, allowing zip1 cells to sporulate. Red1 or Mek1 overproduction also promotes sporulation of other mutants (zip2, dmc1, hop2) that undergo checkpoint-mediated arrest at pachytene. In addition, Red1 overproduction antagonizes interhomolog interactions in thezip1 mutant, substantially decreasing double-strand break formation, meiotic recombination, and homologous chromosome pairing. Mek1 overproduction, in contrast, suppresses checkpoint-induced arrest without significantly decreasing meiotic recombination. Cooverproduction of Red1 and Mek1 fails to bypass the checkpoint; moreover, overproduction of the meiotic chromosomal protein Hop1 blocks the Red1 and Mek1 overproduction phenotypes. These results suggest that meiotic chromosomal proteins function in the signaling of meiotic prophase defects and that the correct stoichiometry of Red1, Mek1, and Hop1 is needed to achieve checkpoint-mediated cell cycle arrest at pachytene.

scholarly journals The Mnd1 Protein Forms a Complex with Hop2 To Promote Homologous Chromosome Pairing and Meiotic Double-Strand Break Repair

2002 ◽  
Vol 22 (9) ◽  
pp. 3078-3088 ◽  
Author(s):  
Hideo Tsubouchi ◽  
G. Shirleen Roeder
Keyword(s):  
Chromosome Pairing ◽  
Meiotic Prophase ◽  
Meiotic Chromosome ◽  
Strand Break ◽  
Rad51 Protein ◽  
Strand Breaks ◽  
Homolog Pairing ◽  
Cell Extracts ◽  
Homologous Chromosome Pairing ◽  
Multicopy Suppressors

ABSTRACT The hop2 mutant of Saccharomyces cerevisiae arrests in meiosis with extensive synaptonemal complex (SC) formation between nonhomologous chromosomes. A screen for multicopy suppressors of a hop2-ts allele identified the MND1 gene. The mnd1-null mutant arrests in meiotic prophase, with most double-strand breaks (DSBs) unrepaired. A low level of mature recombinants is produced, and the Rad51 protein accumulates at numerous foci along chromosomes. SC formation is incomplete, and homolog pairing is severely reduced. The Mnd1 protein localizes to chromatin throughout meiotic prophase, and this localization requires Hop2. Unlike recombination enzymes such as Rad51, Mnd1 localizes to chromosomes even in mutants that fail to initiate meiotic recombination. The Hop2 and Mnd1 proteins coimmunoprecipitate from meiotic cell extracts. These results suggest that Hop2 and Mnd1 work as a complex to promote meiotic chromosome pairing and DSB repair. The identification of Hop2 and Mnd1 homologs in other organisms suggests that the function of this complex is conserved among eukaryotes.

scholarly journals Structural analysis of different LINC complexes reveals distinct binding modes

2020 ◽  
Author(s):  
Victor E. Cruz ◽  
F. Esra Demircioglu ◽  
Thomas U. Schwartz
Keyword(s):  
Structural Analysis ◽  
High Resolution ◽  
Nuclear Envelope ◽  
Chromosome Pairing ◽  
Nuclear Membrane ◽  
Homologous Chromosome ◽  
The Sun ◽  
Binding Modes ◽  
The Core ◽  
Homologous Chromosome Pairing

AbstractLinker of nucleoskeleton and cytoskeleton (LINC) complexes are molecular tethers that span the nuclear envelope (NE) and physically connect the nucleus to the cytoskeleton. They transmit mechanical force across the NE in processes such as nuclear anchorage, nuclear migration, and homologous chromosome pairing during meiosis. LINC complexes are composed of KASH proteins traversing the outer nuclear membrane, and SUN proteins crossing the inner nuclear membrane. Humans have several SUN- and KASH-containing proteins, yet what governs their proper engagement is poorly understood. To investigate this question, we solved high resolution crystal structures of human SUN2 in complex with the KASH-peptides of Nesprin3, Nesprin4, and KASH5. In comparison to the published structures of SUN2-KASH1/2 we observe alternative binding modes for these KASH peptides. While the core interactions between SUN and the C-terminal residues of the KASH peptide are similar in all five complexes, the extended KASH-peptide adopts at least two different conformations. The much-improved resolution allows for a more detailed analysis of other elements critical for KASH interaction, including the KASH-lid and the cation loop, and a possible self-locked state for unbound SUN. In summary, we observe distinct differences between the examined SUN-KASH complexes. These differences may have an important role in regulating the SUN-KASH network.

Homologous chromosome pairing

1977 ◽  
Vol 277 (955) ◽  
pp. 245-258 ◽  
Keyword(s):  
Synaptonemal Complex ◽  
Chromosome Pairing ◽  
Homologous Chromosome ◽  
Crossing Over ◽  
Supporting Evidence ◽  
Mitotic Metaphase ◽  
Sister Chromatids ◽  
Homologous Chromosome Pairing ◽  
Attachment Sites ◽  
Crossover Site

Commonly accepted precepts are challenged : (1) that homologous chromosome pairing is normally mediated by nuclear envelope attachment sites; (2) that crossover site establishment awaits synaptic completion; and (3) that it is the function of the synaptonemal complex to hold homologues in register so that equal crossing over can occur, and perhaps to provide machinery for the crossover process. Although these views may eventually be shown to be true, it is felt that currently available evidence does not warrant their full acceptance, and that alternatives should be considered. As examples of alternatives the following ideas, with some supporting evidence, are suggested: (1) homologous chromsome pairing (in non-haplont organisms) may be accomplished by chance meeting of homologue segments (followed by establishment of invisible, elastic connectors) at congression for a mitotic metaphase (in many cases perhaps the premeiotic mitosis); (2) crossover sites may be established before, during, or immediately following initiation of synapsis; and (3) the synaptonemal complex may somehow function in the crossover process at the inception of its formation, but its complete deployment throughout each normal bivalent may serve some other role, such as mediation of the binding of sister chromatids apparently required for chiasma maintenance until anaphase I.

scholarly journals Bqt2p is essential for initiating telomere clustering upon pheromone sensing in fission yeast

2006 ◽  
Vol 173 (6) ◽  
pp. 845-851 ◽  
Author(s):  
Xie Tang ◽  
Ye Jin ◽  
W. Zacheus Cande
Keyword(s):  
Fission Yeast ◽  
Chromosome Pairing ◽  
Meiotic Prophase ◽  
Homologous Chromosome ◽  
Spindle Pole Body ◽  
Spindle Pole ◽  
Meiotic Spindle ◽  
Meiotic Progression ◽  
Pole Body ◽  
Homologous Chromosome Pairing

The telomere bouquet, i.e., telomere clustering on the nuclear envelope (NE) during meiotic prophase, is thought to promote homologous chromosome pairing. Using a visual screen, we identified bqt2/im295, a mutant that disrupts telomere clustering in fission yeast. Bqt2p is required for linking telomeres to the meiotic spindle pole body (SPB) but not for attachment of telomeres or the SPB to the NE. Bqt2p is expressed upon pheromone sensing and colocalizes thereafter to Sad1p, an SPB protein. This localization only depends on Bqt1p, not on other identified proteins required for telomere clustering. Upon pheromone sensing, generation of Sad1p foci next to telomeres depends on Bqt2p. However, depletion of Bqt2p from the SPB is dispensable for dissolving the telomere bouquet at the end of meiotic prophase. Therefore, telomere bouquet formation requires Bqt2p as a linking component and is finely regulated during meiotic progression.

scholarly journals Dynamics of Homologous Chromosome Pairing during Meiotic Prophase in Fission Yeast

2004 ◽  
Vol 6 (3) ◽  
pp. 329-341 ◽  
Author(s):  
Da-Qiao Ding ◽  
Ayumu Yamamoto ◽  
Tokuko Haraguchi ◽  
Yasushi Hiraoka
Keyword(s):  
Fission Yeast ◽  
Chromosome Pairing ◽  
Meiotic Prophase ◽  
Homologous Chromosome ◽  
Homologous Chromosome Pairing

Homologous chromosome pairing in wheat

1999 ◽  
Vol 112 (11) ◽  
pp. 1761-1769 ◽  
Author(s):  
E. Martinez-Perez ◽  
P. Shaw ◽  
S. Reader ◽  
L. Aragon-Alcaide ◽  
T. Miller ◽  
...  
Keyword(s):  
Chromosome Pairing ◽  
Meiotic Prophase ◽  
Homologous Chromosome ◽  
Wild Type ◽  
Sister Chromatids ◽  
Homologous Chromosome Pairing ◽  
Tapetal Cells ◽  
Telomere Cluster ◽  
Diploid Cells ◽  
Degree Of Association

Bread wheat is a hexaploid (AABBDD, 2n=6x=42) containing three related ancestral genomes, each having 7 chromosomes, giving 42 chromosomes in diploid cells. During meiosis true homologues are correctly associated in wild-type wheat, but a degree of association of related chromosomes (homoeologues) occurs in a mutant (ph1b). We show that the centromeres are associated in non-homologous pairs in all floral tissues studied, both in wild-type wheat and the ph1b mutant. The non-homologous centromere associations then become homologous premeiotically in wild-type wheat in both meiocytes and the tapetal cells, but not in the mutant. In wild-type wheat, the homologues are colocalised along their length at this stage, but the telomeres remain distinct. A single telomere cluster (bouquet) is formed in the meiocytes only by the onset of leptotene. The sub-telomeric regions of the homologues associate as the telomere cluster forms. The homologous associations at the telomeres and centromeres are maintained through meiotic prophase, although, during leptotene, the two homologues and also the sister chromatids within each homologue are separate along the rest of their length. As meiosis progresses, first the sister chromatids and then the homologues associate intimately. In wild-type wheat, first the centromere grouping, then the bouquet disperse by the end of zygotene.

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