scholarly journals Identification of Novel Drosophila Meiotic Genes Recovered in a P-Element Screen

Genetics ◽  
1999 ◽  
Vol 152 (2) ◽  
pp. 529-542 ◽  
Author(s):  
Jeff J Sekelsky ◽  
Kim S McKim ◽  
Lisa Messina ◽  
Rachael L French ◽  
Wendy D Hurley ◽  
...  
Keyword(s):  
Genetic Background ◽  
Meiotic Chromosome ◽  
Structure And Function ◽  
P Element ◽  
Meiotic Spindle ◽  
High Fidelity ◽  
Crossing Over ◽  
Wild Type ◽  
Homologous Chromosomes ◽  
And Function

Abstract The segregation of homologous chromosomes from one another is the essence of meiosis. In many organisms, accurate segregation is ensured by the formation of chiasmata resulting from crossing over. Drosophila melanogaster females use this type of recombination-based system, but they also have mechanisms for segregating achiasmate chromosomes with high fidelity. We describe a P-element mutagenesis and screen in a sensitized genetic background to detect mutations that impair meiotic chromosome pairing, recombination, or segregation. Our screen identified two new recombination-deficient mutations: mei-P22, which fully eliminates meiotic recombination, and mei-P26, which decreases meiotic exchange by 70% in a polar fashion. We also recovered an unusual allele of the ncd gene, whose wild-type product is required for proper structure and function of the meiotic spindle. However, the screen yielded primarily mutants specifically defective in the segregation of achiasmate chromosomes. Although most of these are alleles of previously undescribed genes, five were in the known genes αTubulin67C, CycE, push, and Trl. The five mutations in known genes produce novel phenotypes for those genes.

scholarly journals The Role of Centromere Alignment in Meiosis I Segregation of Homologous Chromosomes in Saccharomyces cerevisiae

Genetics ◽  
1999 ◽  
Vol 153 (4) ◽  
pp. 1547-1560
Author(s):  
Cesar E Guerra ◽  
David B Kaback
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Chromosome Segregation ◽  
Meiotic Chromosome ◽  
Meiotic Spindle ◽  
Physical Interaction ◽  
Crossing Over ◽  
Homologous Chromosomes ◽  
Chromosome Alignment ◽  
Chromosome I

AbstractDuring meiosis, homologous chromosomes pair and then segregate from each other at the first meiotic division. Homologous centromeres appear to be aligned when chromosomes are paired. The role of centromere alignment in meiotic chromosome segregation was investigated in Saccharomyces cerevisiae diploids that contained one intact copy of chromosome I and one copy bisected into two functional centromere-containing fragments. The centromere on one fragment was aligned with the centromere on the intact chromosome while the centromere on the other fragment was either aligned or misaligned. Fragments containing aligned centromeres segregated efficiently from the intact chromosome, while fragments containing misaligned centromeres segregated much less efficiently from the intact chromosome. Less efficient segregation was correlated with crossing over in the region between the misaligned centromeres. Models that suggest that these crossovers impede proper segregation by preventing either a segregation-promoting chromosome alignment on the meiotic spindle or some physical interaction between homologous centromeres are proposed.

scholarly journals SID1-1: a mutation affecting meiotic sister-chromatid association in yeast.

Genetics ◽  
1993 ◽  
Vol 134 (2) ◽  
pp. 423-433
Author(s):  
M Flatters ◽  
D Dawson
Keyword(s):  
Chromosome Segregation ◽  
Sister Chromatid ◽  
Meiotic Chromosome ◽  
High Fidelity ◽  
Wild Type ◽  
Homologous Chromosomes ◽  
Marked Chromosome ◽  
Chromosome Iii ◽  
Dominant Mutants ◽  
Meiosis I

Abstract Meiotic chromosome segregation must occur with high fidelity in order to prevent the generation of deleterious aneuploidies. In meiosis I, homologous chromosomes pair, then migrate to opposite poles of the spindle. This process uses a collection of unique structures and mechanisms that have yet to be thoroughly characterized. To acquire a collection of informative meiotic mutants, we carried out a novel genetic screen in Saccharomyces cerevisiae. This screen was designed to identify dominant mutants in which meiosis I chromosome segregation occurs with decreased fidelity. One mutant recovered using this screen, SID1-1 (sister disjunction), showed an incidence of spores disomic for a marked chromosome III that was 25-fold greater than the wild-type level. Crossing-over is slightly, but not dramatically, reduced in SID1-1. Both recombinant and nonrecombinant chromosomes segregate with reduced fidelity in the presence of SID1-1. We present evidence that the mutant is defective in sister-chromatid association.

scholarly journals A Rubisco-binding protein is required for normal pyrenoid number and starch sheath morphology inChlamydomonas reinhardtii

2019 ◽  
Vol 116 (37) ◽  
pp. 18445-18454 ◽  
Author(s):  
Alan K. Itakura ◽  
Kher Xing Chan ◽  
Nicky Atkinson ◽  
Leif Pallesen ◽  
Lianyong Wang ◽  
...  
Keyword(s):  
Surface Area ◽  
Structure And Function ◽  
Binding Motif ◽  
Starch Granules ◽  
Wild Type ◽  
Bisphosphate Carboxylase ◽  
Biophysical Mechanism ◽  
Mechanism Function ◽  
And Function

A phase-separated, liquid-like organelle called the pyrenoid mediates CO2fixation in the chloroplasts of nearly all eukaryotic algae. While most algae have 1 pyrenoid per chloroplast, here we describe a mutant in the model algaChlamydomonasthat has on average 10 pyrenoids per chloroplast. Characterization of the mutant leads us to propose a model where multiple pyrenoids are favored by an increase in the surface area of the starch sheath that surrounds and binds to the liquid-like pyrenoid matrix. We find that the mutant’s phenotypes are due to disruption of a gene, which we call StArch Granules Abnormal 1 (SAGA1) because starch sheath granules, or plates, in mutants lacking SAGA1 are more elongated and thinner than those of wild type. SAGA1 contains a starch binding motif, suggesting that it may directly regulate starch sheath morphology. SAGA1 localizes to multiple puncta and streaks in the pyrenoid and physically interacts with the small and large subunits of the carbon-fixing enzyme Rubisco (ribulose-1,5-bisphosphate carboxylase/oxygenase), a major component of the liquid-like pyrenoid matrix. Our findings suggest a biophysical mechanism by which starch sheath morphology affects pyrenoid number and CO2-concentrating mechanism function, advancing our understanding of the structure and function of this biogeochemically important organelle. More broadly, we propose that the number of phase-separated organelles can be regulated by imposing constraints on their surface area.

scholarly journals Alterations in flight muscle ultrastructure and function in Drosophila tropomyosin mutants.

1996 ◽  
Vol 135 (3) ◽  
pp. 673-687 ◽  
Author(s):  
A J Kreuz ◽  
A Simcox ◽  
D Maughan
Keyword(s):  
Amino Acid ◽  
Power Output ◽  
Flight Muscle ◽  
Structure And Function ◽  
Wild Type ◽  
Muscle Tropomyosin ◽  
Ultrastructure And Function ◽  
And Function ◽  
Net Power Output ◽  
Current Report

Drosophila indirect flight muscle (IFM) contains two different types of tropomyosin: a standard 284-amino acid muscle tropomyosin, Ifm-TmI, encoded by the TmI gene, and two > 400 amino acid tropomyosins, TnH-33 and TnH-34, encoded by TmII. The two IFM-specific TnH isoforms are unique tropomyosins with a COOH-terminal extension of approximately 200 residues which is hydrophobic and rich in prolines. Previous analysis of a hypomorphic TmI mutant, Ifm(3)3, demonstrated that Ifm-TmI is necessary for proper myofibrillar assembly, but no null TmI mutant or TmII mutant which affects the TnH isoforms have been reported. In the current report, we show that four flightless mutants (Warmke et al., 1989) are alleles of TmI, and characterize a deficiency which deletes both TmI and TmII. We find that haploidy of TmI causes myofibrillar disruptions and flightless behavior, but that haploidy of TmII causes neither. Single fiber mechanics demonstrates that power output is much lower in the TmI haploid line (32% of wild-type) than in the TmII haploid line (73% of wild-type). In myofibers nearly depleted of Ifm-TmI, net power output is virtually abolished (< 1% of wild-type) despite the presence of an organized fibrillar core (approximately 20% of wild-type). The results suggest Ifm-TmI (the standard tropomyosin) plays a key role in fiber structure, power production, and flight, with reduced Ifm-TmI expression producing corresponding changes of IFM structure and function. In contrast, reduced expression of the TnH isoforms has an unexpectedly mild effect on IFM structure and function.

scholarly journals The Arabidopsis HOP2 Gene Has a Role in Preventing illegitimate Exchanges between Nonhomologous Chromosomes

2021 ◽  
Author(s):  
YIsell Farahani-Tafreshi ◽  
Chun Wei ◽  
Peilu Gan ◽  
Jenya Daradur ◽  
C. Daniel Riggs ◽  
...  
Keyword(s):  
Active Role ◽  
Crossing Over ◽  
Wild Type ◽  
Positive Role ◽  
Homologous Chromosomes ◽  
Chromosome Synapsis ◽  
Radiation Induced ◽  
Nonhomologous Chromosome ◽  
Chromosome Exchanges

Meiotic homologous chromosomes pair up and undergo crossing over. In many eukaryotes both intimate pairing and crossing over require the induction of double stranded breaks (DSBs) and subsequent repair via Homologous Recombination (HR). In these organisms, two key proteins are the recombinases RAD51 and DMC1. Recombinase-modulators HOP2 and MND1 have been identified as proteins that assist RAD51 and DMC1 and are needed to promote stabilized pairing. We have probed the nature of the genetic lesions seen in hop2 mutants and looked at the role of HOP2 in the fidelity of genetic exchanges. Using γH2AX as a marker for unrepaired DSBs we found that hop2-1 and mnd1 mutants have different appearance/disappearance for DSBs than wild type, but all DSBs are repaired by mid-late pachytene. Therefore, the bridges and fragments seen from metaphase I onward are due to mis-repaired DSBs, not unrepaired ones. Studying Arabidopsis haploid meiocytes we found that wild type haploids produced the expected five univalents, but hop2-1 haploids suffered many illegitimate exchanges that were stable enough to produce bridged chromosomes during segregation. Our results suggest that HOP2 has a significant active role in preventing nonhomologous associations. We also found evidence that HOP2 plays a role in preventing illegitimate exchanges during repair of radiation-induced DSBs in rapidly dividing petal cells. Thus, HOP2 plays both a positive role in promoting homologous chromosome synapsis and a separable role in preventing nonhomologous chromosome exchanges. Possible mechanisms for this second important role are discussed.

scholarly journals The plant circadian clock influences rhizosphere community structure and function

2017 ◽  
Author(s):  
Charley J. Hubbard ◽  
Marcus T. Brock ◽  
Linda T.A. van Diepen ◽  
Loïs Maignien ◽  
Brent E. Ewers ◽  
...  
Keyword(s):  
Community Structure ◽  
Microbial Community ◽  
Circadian Clock ◽  
Structure And Function ◽  
Plant Performance ◽  
Wild Type ◽  
Night Time ◽  
History Of ◽  
And Function ◽  
Rhizosphere Community

AbstractPlants alter chemical and physical properties of soil, and thereby influence rhizosphere microbial community structure. The structure of microbial communities may in turn affect plant performance. Yet, outside of simple systems with pairwise interacting partners, the plant genetic pathways that influence microbial community structure remain largely unknown, as are the performance feedbacks of microbial communities selected by the host plant genotype. We investigated the role of the plant circadian clock in shaping rhizosphere community structure and function. We performed 16S rRNA gene sequencing to characterize rhizosphere bacterial communities of Arabidopsis thaliana between day and night time points, and tested for differences in community structure between wild-type (Ws) vs. clock mutant (toc1-21, ztl-30) genotypes. We then characterized microbial community function, by growing wild-type plants in soils with an overstory history of Ws, toc1-21 or ztl-30 and measuring plant performance. We observed that rhizosphere community structure varied between day and night time points, and clock misfunction significantly altered rhizosphere communities. Finally, wild-type plants germinated earlier and were larger when inoculated with soils having an overstory history of wild-type in comparison to clock mutant genotypes. Our findings suggest the circadian clock of the plant host influences rhizosphere community structure and function.

Maize meiotic spindles assemble around chromatin and do not require paired chromosomes

1998 ◽  
Vol 111 (23) ◽  
pp. 3507-3515 ◽  
Author(s):  
A. Chan ◽  
W.Z. Cande
Keyword(s):  
Nuclear Envelope ◽  
Higher Plants ◽  
Metaphase Plate ◽  
Meiotic Spindle ◽  
Wild Type ◽  
Homologous Chromosomes ◽  
Nuclear Envelope Breakdown ◽  
Meiotic Spindles ◽  
Meiotic Mutations ◽  
Bipolar Spindles

To understand how the meiotic spindle is formed and maintained in higher plants, we studied the organization of microtubule arrays in wild-type maize meiocytes and three maize meiotic mutants, desynaptic1 (dsy1), desynaptic2 (dsy2), and absence of first division (afd). All three meiotic mutations have abnormal chromosome pairing and produce univalents by diakinesis. Using these three mutants, we investigated how the absence of paired homologous chromosomes affects the assembly and maintenance of the meiotic spindle. Before nuclear envelope breakdown, in wild-type meiocytes, there were no bipolar microtubule arrays. Instead, these structures formed after nuclear envelope breakdown and were associated with the chromosomes. The presence of univalent chromosomes in dsy1, dsy2, and afd meiocytes and of unpaired sister chromatids in the afd meiocytes did not affect the formation of bipolar spindles. However, alignment of chromosomes on the metaphase plate and subsequent anaphase chromosome segregation were perturbed. We propose a model for spindle formation in maize meiocytes in which microtubules initially appear around the chromosomes during prometaphase and then the microtubules self-organize. However, this process does not require paired kinetochores to establish spindle bipolarity.

scholarly journals Muscles of mice deficient in α-sarcoglycan maintain large masses and near control force values throughout the life span

2005 ◽  
Vol 22 (2) ◽  
pp. 244-256 ◽  
Author(s):  
Christina M. Consolino ◽  
Franck Duclos ◽  
Jane Lee ◽  
Roger A. Williamson ◽  
Kevin P. Campbell ◽  
...  
Keyword(s):  
Connective Tissue ◽  
Life Span ◽  
Structure And Function ◽  
Null Mouse ◽  
Control Force ◽  
Wild Type ◽  
Cross Sectional ◽  
Muscle Structure ◽  
And Function

α-Sarcoglycan-deficient ( Sgca-null) mice provide potential for elucidating the pathogenesis of limb girdle muscular dystrophy type 2D (LGMD 2D) as well as for studying the effectiveness of therapeutic strategies. Skeletal muscles of Sgca-null mice demonstrate an early onset of extensive fiber necrosis, degeneration, and regeneration, but the progression of the pathology and the effects on muscle structure and function throughout the life span are not known. Thus the phenotypic accuracy of the Sgca-null mouse as a model of LGMD 2D has not been fully established. To investigate skeletal muscle structure and function in the absence of α-sarcoglycan throughout the life span, we analyzed extensor digitorum longus and soleus muscles of male and female Sgca-null and wild-type mice at 3, 6, 12, and 18 mo of age. Maximum isometric forces and powers were measured in vitro at 25°C. Also determined were individual myofiber cross-sectional areas and numbers, water content, and the proportion of the cross section occupied by connective tissue. Muscle masses were 40–100% larger for Sgca-null compared with age- and gender-matched wild-type mice, with the majority of the increased muscle mass for Sgca-null mice attributable to greater connective tissue and water contents. Although the greater mass of muscles in Sgca-null mice was primarily noncontractile material, absolute forces and powers were maintained near control levels at all ages, indicating a successful adaptation to the deficiency in α-sarcoglycan not observed at any age in LGMD 2D patients.

scholarly journals Gene Families, Epistasis and the Amino Acid Preferences of Protein Homologs

2019 ◽  
Vol 15 ◽  
pp. 117693431987048
Author(s):  
Evandro Ferrada
Keyword(s):  
Amino Acid ◽  
Genetic Background ◽  
Sequence Divergence ◽  
Gene Families ◽  
Structure And Function ◽  
Sequence Evolution ◽  
Systematic Analysis ◽  
Fitness Effects ◽  
Computational Work ◽  
And Function

In order to preserve structure and function, proteins tend to preferentially conserve amino acids at particular sites along the sequence. Because mutations can affect structure and function, the question arises whether the preference of a protein site for a particular amino acid varies between protein homologs, and to what extent that variation depends on sequence divergence. Answering these questions can help in the development of models of sequence evolution, as well as provide insights on the dependence of the fitness effects of mutations on the genetic background of sequences, a phenomenon known as epistasis. Here, I comment on recent computational work providing a systematic analysis of the extent to which the amino acid preferences of proteins depend on the background mutations of protein homologs.

The Structure and Function of Murine Factor V and Its Inactivation by Protein C

Blood ◽  
1998 ◽  
Vol 91 (12) ◽  
pp. 4593-4599 ◽  
Author(s):  
Tony L. Yang ◽  
Jisong Cui ◽  
Alnawaz Rehumtulla ◽  
Angela Yang ◽  
Micheline Moussalli ◽  
...  
Keyword(s):  
Amino Acid ◽  
Protein C ◽  
Mammalian Species ◽  
Structure And Function ◽  
Procoagulant Activity ◽  
Factor V ◽  
Cleavage Sites ◽  
Wild Type ◽  
Coding Region ◽  
And Function

Factor V (FV) is a central regulator of hemostasis, serving both as a critical cofactor for the prothrombinase activity of factor Xa and the target for proteolytic inactivation by the anticoagulant, activated protein C (APC). To examine the evolutionary conservation of FV procoagulant activity and functional inactivation by APC, we cloned and sequenced the coding region of murine FV cDNA and generated recombinant wild-type and mutant murine FV proteins. The murine FV cDNA encodes a 2,183-amino acid protein. Sequence comparison shows that the A1-A3 and C1-C2 domains of FV are highly conserved, demonstrating greater than 84% sequence identity between murine and human, and 60% overall amino acid identity among human, bovine, and murine FV sequences. In contrast, only 35% identity among all three species is observed for the poorly conserved B domain. The arginines at all thrombin cleavage sites and the R305 and R504 APC cleavage sites (corresponding to amino acid residues R306 and R506 in human FV) are invariant in all three species. Point mutants were generated to substitute glutamine at R305, R504, or both (R305/R504). Wild-type and all three mutant FV recombinant proteins show equivalent FV procoagulant activity. Single mutations at R305 or R504 result in partial resistance of FV to APC inactivation, whereas recombinant murine FV carrying both mutations (R305Q/R504Q) is nearly completely APC resistant. Thus, the structure and function of FV and its interaction with APC are highly conserved across mammalian species.

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