scholarly journals Meiotic shugoshins differ from mitotic ones by arginine-reach C-terminal motif in yeast, plant, animals, and human

2016 ◽  
Author(s):  
Tatiana M Grishaeva ◽  
Darya Kulichenko ◽  
Yuri F Bogdanov
Keyword(s):  
Amino Acid ◽  
Structural Difference ◽  
Protein Molecule ◽  
Meiotic Metaphase ◽  
Chromosome Behavior ◽  
Sister Chromatids ◽  
Arginine Residues ◽  
The Difference ◽  
Mitosis And Meiosis ◽  
Metaphase I

Background. Shugoshins (SGOs) are proteins that protect cohesins located at the centromeres of sister chromatids from their early cleavage during mitosis and meiosis in plants, fungi, and animals. Their function is to prevent premature sister-chromatid disjunction and segregation. Meiotic SGOs prevent segregation of sister chromatids in meiosis I, thus permitting homologous chromosomes to segregate and reduce chromosome number to haploid set. The study focused on the structural differences among shugoshins acting during mitosis and meiosis that cause differences in chromosome behavior in these two types of cell division in different organisms. Methods. A bioinformatics analysis of protein domains, conserved amino acid motifs, and physicochemical properties of 32 proteins from 25 species of plants, fungi, and animals was performed. Results. We identified a C-terminal arginine-reach amino acid motif that is highly evolutionarily conserved among the shugoshins protecting centromere cohesion of sister chromatids in meiotic anaphase I, but not among mitotic shugoshins. The motif looks like “arginine comb” capable of interaction by hydrogen bonds with guanine bases in the small groove of DNA helix. Shugoshins in different eukaryotic kingdoms differ also in the sets and location of amino acid motifs and the number of α-helical regions in the protein molecule. Discussion. Meiosis-specific arginine-reach motif may be responsible for formation of SGO-DNA nucleoprotein complex, thus protecting meiotic shugoshins from degradation during meiotic metaphase I and anaphase I, while mitotic SGOs have a motif with less number of arginine residues. This structural difference between meiotic and mitotic shugoshins, probably, could be a key molecular element of the prolonged shugoshin resistance to degradation during meiotic metaphase I and anaphase I and be one of the molecular elements causing the difference in chromosome behavior in meiosis and mitosis. The finding of differences in SGO structure in plant, fungi and animals supports idea of independent evolution of meiosis in different lineages of multicellular organisms.

scholarly journals Meiotic shugoshins differ from mitotic ones by arginine-reach C-terminal motif in yeast, plant, animals, and human

2016 ◽  
Author(s):  
Tatiana M Grishaeva ◽  
Darya Kulichenko ◽  
Yuri F Bogdanov
Keyword(s):  
Amino Acid ◽  
Structural Difference ◽  
Protein Molecule ◽  
Meiotic Metaphase ◽  
Chromosome Behavior ◽  
Sister Chromatids ◽  
Arginine Residues ◽  
The Difference ◽  
Mitosis And Meiosis ◽  
Metaphase I

Background. Shugoshins (SGOs) are proteins that protect cohesins located at the centromeres of sister chromatids from their early cleavage during mitosis and meiosis in plants, fungi, and animals. Their function is to prevent premature sister-chromatid disjunction and segregation. Meiotic SGOs prevent segregation of sister chromatids in meiosis I, thus permitting homologous chromosomes to segregate and reduce chromosome number to haploid set. The study focused on the structural differences among shugoshins acting during mitosis and meiosis that cause differences in chromosome behavior in these two types of cell division in different organisms. Methods. A bioinformatics analysis of protein domains, conserved amino acid motifs, and physicochemical properties of 32 proteins from 25 species of plants, fungi, and animals was performed. Results. We identified a C-terminal arginine-reach amino acid motif that is highly evolutionarily conserved among the shugoshins protecting centromere cohesion of sister chromatids in meiotic anaphase I, but not among mitotic shugoshins. The motif looks like “arginine comb” capable of interaction by hydrogen bonds with guanine bases in the small groove of DNA helix. Shugoshins in different eukaryotic kingdoms differ also in the sets and location of amino acid motifs and the number of α-helical regions in the protein molecule. Discussion. Meiosis-specific arginine-reach motif may be responsible for formation of SGO-DNA nucleoprotein complex, thus protecting meiotic shugoshins from degradation during meiotic metaphase I and anaphase I, while mitotic SGOs have a motif with less number of arginine residues. This structural difference between meiotic and mitotic shugoshins, probably, could be a key molecular element of the prolonged shugoshin resistance to degradation during meiotic metaphase I and anaphase I and be one of the molecular elements causing the difference in chromosome behavior in meiosis and mitosis. The finding of differences in SGO structure in plant, fungi and animals supports idea of independent evolution of meiosis in different lineages of multicellular organisms.

scholarly journals Bioinformatical analysis of eukaryotic shugoshins reveals meiosis-specific features of vertebrate shugoshins

PeerJ ◽  
2016 ◽  
Vol 4 ◽  
pp. e2736 ◽  
Author(s):  
Tatiana M. Grishaeva ◽  
Darya Kulichenko ◽  
Yuri F. Bogdanov
Keyword(s):  
Amino Acid ◽  
Protein Molecule ◽  
Early Cleavage ◽  
Sister Chromatids ◽  
Evolutionarily Conserved ◽  
Bioinformatical Analysis ◽  
Structural Differences ◽  
Terminal Amino ◽  
Multicellular Organisms ◽  
Mitosis And Meiosis

BackgroundShugoshins (SGOs) are proteins that protect cohesins located at the centromeres of sister chromatids from their early cleavage during mitosis and meiosis in plants, fungi, and animals. Their function is to prevent premature sister-chromatid disjunction and segregation. The study focused on the structural differences among SGOs acting during mitosis and meiosis that cause differences in chromosome behavior in these two types of cell division in different organisms.MethodsA bioinformatical analysis of protein domains, conserved amino acid motifs, and physicochemical properties of 32 proteins from 25 species of plants, fungi, and animals was performed.ResultsWe identified a C-terminal amino acid motif that is highly evolutionarily conserved among the SGOs protecting centromere cohesion of sister chromatids in meiotic anaphase I, but not among mitotic SGOs. This meiotic motif is arginine-rich in vertebrates. SGOs differ in different eukaryotic kingdoms by the sets and locations of amino acid motifs and the number of α-helical regions in the protein molecule.DiscussionThese structural differences between meiotic and mitotic SGOs probably could be responsible for the prolonged SGOs resistance to degradation during meiotic metaphase I and anaphase I. We suggest that the “arginine comb” in C-end meiotic motifs is capable of interaction by hydrogen bonds with guanine bases in the minor groove of DNA helix, thus protecting SGOs from hydrolysis. Our findings support independent evolution of meiosis in different lineages of multicellular organisms.

Presence of a centromeric filament during meiosis

Genome ◽  
1991 ◽  
Vol 34 (6) ◽  
pp. 888-894 ◽  
Author(s):  
Alberto J. Solari ◽  
Carlos J. Tandler
Keyword(s):  
Synaptonemal Complex ◽  
Staining Technique ◽  
Meiotic Metaphase ◽  
Mitotic Chromosomes ◽  
Intense Staining ◽  
Lateral Element ◽  
Centromeric Chromatin ◽  
Sister Chromatids ◽  
Silver Staining Technique ◽  
Metaphase I

Spermatocytes at meiotic metaphase I and anaphase I have a characteristic centromeric filament in a variety of vertebrate organisms. This centromeric filament was first demonstrated on mouse spermatocytes and its presence is now extended to spermatocytes from the human, rat, golden hamster, bull, and chicken. The visualization of this filament was possible through the use of a novel silver-staining technique, which allows a high contrast between the filament and the centromeric chromatin. In the species cited, the centromeric filament shares an intense staining, a short (0.2–0.6 μm) length, a curved and branched shape, and location inside the centromeric chromatin of seemingly every homologue of the complement. The similarity of staining reactivity and the observation of transitional structures during first meiotic prophase strongly suggest that the centromeric filament is a remnant of a lateral element of the synaptonemal complex, which stays specifically at both centromeric regions of each bivalent. This filament is not found at the second meiotic division or at the centromeres of mitotic chromosomes. It is assumed that this centromeric filament joins the two sister chromatids of each homologue at the centromere and thus ensures the proper coorientation of sister kinetochores at metaphase I. Further testable assumptions on the functions of this filament are presented.Key words: synaptonemal complex, meiosis, meiotic centromeres.

scholarly journals Data mining of coronavirus: SARS-CoV-2, SARS-CoV and MERS-CoV

2021 ◽  
Vol 14 (1) ◽  
Author(s):  
Jung Eun Huh ◽  
Seunghee Han ◽  
Taeseon Yoon
Keyword(s):  
Machine Learning ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Decision Tree ◽  
Machine Learning Algorithms ◽  
High Similarity ◽  
Incubation Periods ◽  
Initial Question ◽  
The Difference ◽  
Blast Program

Abstract Objective In this study we compare the amino acid and codon sequence of SARS-CoV-2, SARS-CoV and MERS-CoV using different statistics programs to understand their characteristics. Specifically, we are interested in how differences in the amino acid and codon sequence can lead to different incubation periods and outbreak periods. Our initial question was to compare SARS-CoV-2 to different viruses in the coronavirus family using BLAST program of NCBI and machine learning algorithms. Results The result of experiments using BLAST, Apriori and Decision Tree has shown that SARS-CoV-2 had high similarity with SARS-CoV while having comparably low similarity with MERS-CoV. We decided to compare the codons of SARS-CoV-2 and MERS-CoV to see the difference. Though the viruses are very alike according to BLAST and Apriori experiments, SVM proved that they can be effectively classified using non-linear kernels. Decision Tree experiment proved several remarkable properties of SARS-CoV-2 amino acid sequence that cannot be found in MERS-CoV amino acid sequence. The consequential purpose of this paper is to minimize the damage on humanity from SARS-CoV-2. Hence, further studies can be focused on the comparison of SARS-CoV-2 virus with other viruses that also can be transmitted during latent periods.

scholarly journals Genes Involved in Sister Chromatid Separation and Segregation in the Budding Yeast Saccharomyces cerevisiae

Genetics ◽  
2001 ◽  
Vol 159 (2) ◽  
pp. 453-470
Author(s):  
Sue Biggins ◽  
Needhi Bhalla ◽  
Amy Chang ◽  
Dana L Smith ◽  
Andrew W Murray
Keyword(s):  
Chromosome Segregation ◽  
Sister Chromatid ◽  
Mitotic Spindle ◽  
Budding Yeast ◽  
Temperature Sensitive ◽  
Chromosome Behavior ◽  
Yeast Saccharomyces Cerevisiae ◽  
Sister Chromatids ◽  
Marked Chromosome ◽  
Sister Chromatid Separation

Abstract Accurate chromosome segregation requires the precise coordination of events during the cell cycle. Replicated sister chromatids are held together while they are properly attached to and aligned by the mitotic spindle at metaphase. At anaphase, the links between sisters must be promptly dissolved to allow the mitotic spindle to rapidly separate them to opposite poles. To isolate genes involved in chromosome behavior during mitosis, we microscopically screened a temperature-sensitive collection of budding yeast mutants that contain a GFP-marked chromosome. Nine LOC (loss of cohesion) complementation groups that do not segregate sister chromatids at anaphase were identified. We cloned the corresponding genes and performed secondary tests to determine their function in chromosome behavior. We determined that three LOC genes, PDS1, ESP1, and YCS4, are required for sister chromatid separation and three other LOC genes, CSE4, IPL1, and SMT3, are required for chromosome segregation. We isolated alleles of two genes involved in splicing, PRP16 and PRP19, which impair α-tubulin synthesis thus preventing spindle assembly, as well as an allele of CDC7 that is defective in DNA replication. We also report an initial characterization of phenotypes associated with the SMT3/SUMO gene and the isolation of WSS1, a high-copy smt3 suppressor.

Single amino acid substitution of rat MRP2 results in acquired transport activity for taurocholate

2001 ◽  
Vol 281 (4) ◽  
pp. G1034-G1043 ◽  
Author(s):  
Kousei Ito ◽  
Hiroshi Suzuki ◽  
Yuichi Sugiyama
Keyword(s):  
Amino Acids ◽  
Multidrug Resistance ◽  
Amino Acid ◽  
Membrane Vesicles ◽  
Single Amino Acid ◽  
Sf9 Cells ◽  
Transport Activity ◽  
Wild Type ◽  
Cationic Amino Acids ◽  
The Difference

Multidrug resistance-associated protein 3 (MRP3), unlike other MRPs, transports taurocholate (TC). The difference in TC transport activity between rat MRP2 and MRP3 was studied, focusing on the cationic amino acids in the transmembrane domains. For analysis, transport into membrane vesicles from Sf9 cells expressing wild-type and mutated MRP2 was examined. Substitution of Arg at position 586 with Leu and Ile and substitution of Arg at position 1096 with Lys, Leu, and Met resulted in the acquisition of TC transport activity, while retaining transport activity for glutathione and glucuronide conjugates. Substitution of Leu at position 1084 of rat MRP3 (which corresponds to Arg-1096 in rat MRP2) with Lys, but not with Val or Met, resulted in the loss of transport activity for TC and glucuronide conjugates. These results suggest that the presence of the cationic charge at Arg-586 and Arg-1096 in rat MRP2 prevents the transport of TC, whereas the presence of neutral amino acids at the corresponding position of rat MRP3 is required for the transport of substrates.

Influence of Blood Group and Secretor Status on Carbohydrate Structures in Human Gastric Mucins: Implications for Peptic Ulcer

1995 ◽  
Vol 89 (4) ◽  
pp. 405-415 ◽  
Author(s):  
R. L. Sidebotham ◽  
J. H. Baron ◽  
J. Schrager ◽  
J. Spencer ◽  
J. R. Clamp ◽  
...  
Keyword(s):  
Peptic Ulcer ◽  
Amino Acid ◽  
Blood Group ◽  
Average Length ◽  
Amino Acid Residues ◽  
Secretor Status ◽  
Increased Risk ◽  
The Mean ◽  
The Difference ◽  
Carbohydrate Chains

1. The content and distribution of carbohydrate was examined in mucus glycopolypeptides from human antral mucosae. 2. The mean amount of carbohydrate per 1000 amino acid residues was found to be similar in glycopolypeptides with A, B or H activity. It was slightly, though significantly, less in glycopolypeptides lacking these determinants, because carbohydrate chains were of a shorter average length than in the A-, B- or H-active preparations. This difference was reflected in the sizes of oligosaccharide—alcohols released from representative glycopolypeptides with alkaline borohydride. 3. Differences between A-, B- or H-active and non-secretor glycopolypeptides in terms of the mean number of carbohydrate chains per 1000 amino acid residues were found to be small, and without significance. 4. The average number of peripheral monosaccharide units per 1000 amino acid residues was greater in A-active than in H-active, and least in non-secretor, glycopolypeptides. This order was reversed for monosaccharide units incorporated into skeletal (core plus backbone) structures. The difference in each case was statistically significant. 5. These findings suggest that the increased risk of peptic ulcer associated with blood group O and non-secretor status is unlikely to be attributable to an inherent deficiency in the protective mucus layer, linked to differences between mucins that are associated with A, B or H activity. Other hypotheses linked to infection with Helicobacter pylori are examined.

scholarly journals Phenylalanine requirement in children with classical PKU determined by indicator amino acid oxidation

2002 ◽  
Vol 283 (6) ◽  
pp. E1249-E1256 ◽  
Author(s):  
Glenda Courtney-Martin ◽  
Rachelle Bross ◽  
Mahroukh Raffi ◽  
Joe T. R. Clarke ◽  
Ronald O. Ball ◽  
...  
Keyword(s):  
Amino Acid ◽  
Acid Oxidation ◽  
Phenylalanine Concentration ◽  
Two Phase ◽  
Amino Acid Oxidation ◽  
Blood Phenylalanine ◽  
Plasma Phenylalanine ◽  
Crossover Analysis ◽  
The Mean ◽  
The Difference

Dietary restriction of phenylalanine is the main treatment for phenylketonuria (PKU), and current estimates of requirements are based on plasma phenylalanine concentration and growth. The present study aimed to determine more precisely the phenylalanine requirements in patients with the disease by use of indicator amino acid oxidation, withl-[1-13C]lysine as the indicator. Breath13CO2 production (F13 co 2) was used as the end point. Finger-prick blood samples were also collected for measurement of phenylalanine to relate phenylalanine intake to blood phenylalanine levels. The mean phenylalanine requirement, estimated using a two-phase linear regression crossover analysis, was 14 mg · kg−1 · day−1, and the safe population intake (upper 95% confidence interval of the mean) was found to be 19.5 mg · kg−1 · day−1. A balance between phenylalanine intake and the difference between fed and fasted blood phenylalanine concentration was observed at an intake of 20 mg · kg−1 · day−1. The similarity between these two values (19.5 and 20 mg · kg−1 · day−1) suggests that the maximal phenylalanine intake for children with PKU should be no higher than 20 mg · kg−1 · day−1.

scholarly journals WRAP-based nanoparticles for siRNA delivery: a SAR study and a comparison with lipid-based transfection reagents

2021 ◽  
Vol 19 (1) ◽  
Author(s):  
Karidia Konate ◽  
Emilie Josse ◽  
Milana Tasic ◽  
Karima Redjatti ◽  
Gudrun Aldrian ◽  
...  
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Gene Silencing ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Sirna Delivery ◽  
Cell Penetrating Peptides ◽  
Sirna Transfection ◽  
Arginine Residues ◽  
Sar Study

AbstractRecently, we designed novel amphipathic cell-penetrating peptides, called WRAP, able to transfer efficiently siRNA molecules into cells. In order to gain more information about the relationship between amino acid composition, nanoparticle formation and cellular internalization of these peptides composed of only three amino acids (leucine, arginine and tryptophan), we performed a structure–activity relationship (SAR) study. First, we compared our WRAP1 and WRAP5 peptides with the C6M1 peptide also composed of the same three amino acids and showing similar behaviors in siRNA transfection. Afterwards, to further define the main determinants in the WRAP activity, we synthesized 13 new WRAP analogues harboring different modifications like the number and location of leucine and arginine residues, the relative location of tryptophan residues, as well as the role of the α-helix formation upon proline insertions within the native WRAP sequence. After having compared the ability of these peptides to form peptide-based nanoparticles (PBNs) using different biophysical methods and to induce a targeted gene silencing in cells, we established the main sequential requirements of the amino acid composition of the WRAP peptide. In addition, upon measuring the WRAP-based siRNA transfection ability into cells compared to several non-peptide transfection agents available on the markets, we confirmed that WRAP peptides induced an equivalent level of targeted gene silencing but in most of the cases with lower cell toxicity as clearly shown in clonogenic assays.

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