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.

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 Solid-State and Solution-Phase Conformations of Pseudoproline-Containing Dipeptides

2009 ◽  
Vol 62 (7) ◽  
pp. 711 ◽  
Author(s):  
Jack K. Clegg ◽  
James R. Cochrane ◽  
Nima Sayyadi ◽  
Danielle Skropeta ◽  
Peter Turner ◽  
...  
Keyword(s):  
Amino Acid ◽  
Solid State ◽  
Crystal Packing ◽  
Amide Bond ◽  
Side Chain ◽  
Trans Conformation ◽  
N Terminus ◽  
Structural Differences ◽  
Terminal Amino ◽  
Packing Interactions

The conformations of 14 threonine-derived pseudoproline-containing dipeptides (including four d-allo-Thr derivatives) have been investigated by NMR. In solution, the major conformer observed for all dipeptides is that in which the amide bond between the pseudoproline and the preceding amino acid is cis. For dipeptides in which the N-terminus is protected, the ratio of cis- to trans-conformers does not depend significantly on the side chain of the N-terminal amino acid, or the stereochemistry of the Thr residue. However, for dipeptides bearing a free N-terminus, there are significant differences in the ratios of cis- to trans-conformers depending on the side chain present. Three dipeptides were crystallized and their X-ray structures determined. In two cases, (benzyloxycarbonyl (Cbz)-Val-Thr(ΨMe,Mepro)-OMe and Cbz-Val-Thr(ΨMe,Mepro)-OH), the dipeptides adopt a trans-conformation in the solid state, in contrast to the structures observed in solution. In the third case, (9-fluorenylmethoxycarbonyl (Fmoc)-Val-d-allo-Thr(ΨMe,Mepro)-OH), a cis-amide geometry is observed. These structural differences are attributed to crystal-packing interactions.

scholarly journals Structural differences between two lectins from Cytisus scoparius, both specific for D-galactose and N-acetyl-D-galactosamine

1984 ◽  
Vol 222 (1) ◽  
pp. 41-48 ◽  
Author(s):  
N M Young ◽  
D C Watson ◽  
R E Williams
Keyword(s):  
Amino Acid ◽  
Leguminous Plant ◽  
Cytisus Scoparius ◽  
Terminal Amino Acid ◽  
The Third ◽  
Scotch Broom ◽  
Structural Differences ◽  
Terminal Amino ◽  
Polypeptide Chains ◽  
Terminal Amino Acid Sequence

Three lectin fractions were obtained from seeds of the leguminous plant Cytisus scoparius (Scotch broom) by means of affinity chromatography on a N-acetyl-D-galactosamine medium. The first fraction, termed CSIa, was equally well inhibited in haemagglutination experiments by D-galactose and by N-acetyl-D-galactosamine and consisted of a group of isolectins formed from closely related polypeptide chains of approx. Mr 30000. The second fraction, CSIb, was closely related to CSIa in specificity, c.d. and other properties. The third fraction contained a homogeneous lectin, CSII, formed from subunits again of approx. Mr 30000. CSII was 100 times more readily inhibited by N-acetyl-D-galactosamine than by D-galactose. Despite the similarity in specificity, comparative studies of their amino acid composition, c.d. and N-terminal amino acid sequence showed that the CSIa and CSII lectins diverged considerably in structure. The lectin from Cytisus sessilifolius, specific for chitobiose, was also examined and resembled CSIa in composition and c.d. properties.

Immunoelectron microscope detection of C-type natriuretic peptide in normal human atrial tissue

1993 ◽  
Vol 51 ◽  
pp. 388-389
Author(s):  
Chi-Ming Wei ◽  
Margaret Hukee ◽  
Christopher G.A. McGregor ◽  
John C. Burnett
Keyword(s):  
Amino Acid ◽  
Natriuretic Peptide ◽  
Vascular Tone ◽  
Cardiac Tissue ◽  
Ring Structure ◽  
Terminal Amino Acid ◽  
Amino Acid Peptide ◽  
Normal Human ◽  
Terminal Amino ◽  
The Brain

C-type natriuretic peptide (CNP) is a newly identified peptide that is structurally related to atrial (ANP) and brain natriuretic peptide (BNP). CNP exists as a 22-amino acid peptide and like ANP and BNP has a 17-amino acid ring formed by a disulfide bond. Unlike these two previously identified cardiac peptides, CNP lacks the COOH-terminal amino acid extension from the ring structure. ANP, BNP and CNP decrease cardiac preload, but unlike ANP and BNP, CNP is not natriuretic. While ANP and BNP have been localized to the heart, recent investigations have failed to detect CNP mRNA in the myocardium although small concentrations of CNP are detectable in the porcine myocardium. While originally localized to the brain, recent investigations have localized CNP to endothelial cells consistent with a paracrine role for CNP in the control of vascular tone. While CNP has been detected in cardiac tissue by radioimmunoassay, no studies have demonstrated CNP localization in normal human heart by immunoelectron microscopy.

Apoptosis and development

2003 ◽  
Vol 39 ◽  
pp. 11-24 ◽  
Author(s):  
Justin V McCarthy
Keyword(s):  
Drosophila Melanogaster ◽  
Mammalian Cells ◽  
Cell Number ◽  
Model Organisms ◽  
Biological Processes ◽  
Nematode Caenorhabditis Elegans ◽  
Apoptotic Pathway ◽  
Genetic Pathways ◽  
Evolutionarily Conserved ◽  
Multicellular Organisms

Apoptosis is an evolutionarily conserved process used by multicellular organisms to developmentally regulate cell number or to eliminate cells that are potentially detrimental to the organism. The large diversity of regulators of apoptosis in mammalian cells and their numerous interactions complicate the analysis of their individual functions, particularly in development. The remarkable conservation of apoptotic mechanisms across species has allowed the genetic pathways of apoptosis determined in lower species, such as the nematode Caenorhabditis elegans and the fruitfly Drosophila melanogaster, to act as models for understanding the biology of apoptosis in mammalian cells. Though many components of the apoptotic pathway are conserved between species, the use of additional model organisms has revealed several important differences and supports the use of model organisms in deciphering complex biological processes such as apoptosis.

PURIFICATION AND PARTIAL CHEMICAL CHARACTERIZATION OF SHEEP NEUROPHYSIN

1973 ◽  
Vol 74 (2) ◽  
pp. 226-236 ◽  
Author(s):  
Michel Chrétien ◽  
Claude Gilardeau
Keyword(s):  
Amino Acid ◽  
Polyacrylamide Gel Electrophoresis ◽  
Chemical Characterization ◽  
Terminal Amino Acid ◽  
Amino Acid Determination ◽  
Pituitary Glands ◽  
Terminal Amino ◽  
Partial Chemical ◽  
Acid Determination

ABSTRACT A protein isolated from ovine pituitary glands has been purified, and its homogeneity assessed by NH2- and COOH-terminal amino acid determination, ultracentrifugation studies, and polyacrylamide gel electrophoresis after carboxymethylation. Its chemical and immunochemical properties are closely similar to those of beef and pork neurophysins, less similar to those of human neurophysins. It contains no tryptophan (like other neurophysins) or histidine (like all except bovine neurophysin-I and human neurophysins). It has alanine at the NH2-terminus and valine at the COOH-terminus. Its amino acid composition is similar to, but not identical with those of porcine and bovine neurophysins.

C-Terminal amino acid sequence of chicken pepsinogen and its homology with sequences of other acid proteases

1980 ◽  
Vol 45 (4) ◽  
pp. 1144-1154 ◽  
Author(s):  
Miroslav Baudyš ◽  
Helena Keilová ◽  
Vladimír Kostka
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
The Other ◽  
Terminal Sequence ◽  
Terminal Part ◽  
Terminal Amino Acid ◽  
Tryptic Peptides ◽  
Terminal Amino ◽  
High Degree ◽  
Terminal Amino Acid Sequence

To determine the primary structure of the C-terminal part of the molecule of chicken pepsinogen the tryptic, chymotryptic and thermolytic digest of the protein were investigated and peptides derived from this region were sought. These peptides permitted the following 21-residue C-terminal sequence to be determined: ...Ile-Arg-Glu-Tyr-Tyr-Val-Ile-Phe-Asp-Arg-Ala-Asn-Asn-Lys-Val-Gly-Leu-Ser-Pro-Leu-Ser.COOH. A comparison of this structure with the C-terminal sequential regions of the other acid proteases shows a high degree of homology between chicken pepsinogen and these proteases (e.g., the degree of homology with respect to hog pepsinogen and calf prochymosin is about 66%). Additional tryptic peptides, derived from the N-terminal part of the zymogen molecule whose amino acid sequence has been reported before, were also obtained in this study. This sequence was extended by two residues using an overlapping peptide. An ancillary result of this study was the isolation of tryptic peptides derived from other regions of the zymogen molecule.

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