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- Acrosome reaction (2)
- Adaptation (2)
- Globins (2)
- Guanylate cyclase (2)
- Hemoglobin (2)
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- Hypoxia (2)
- Molecular evolution (2)
- Physiological evolution (2)
- Sea star (2)
- <i>Aphelasterias japonica</i> (1)
- <i>Asterias amurensis</i> (1)
- <i>Asterias rubens</i> (1)
- <i>Asterina pectinifera</i> (1)
- <i>Distolasterias nipon</i> (1)
- <i> Asterias forbesi</i> (1)
- Asterias amurensis (1)
- BirA (1)
- Chemotaxis (1)
- Domains (1)
- Egg jelly (1)
- Fertilization (1)
- Holocarboxylase synthetase (1)
- P67 (1)
- Propionyl-CoA carboxylase (1)
- Proteomics (1)
- Species specificity (1)
- Sperm (1)
- Sperm-activating peptide (1)
Articles 1 - 12 of 12
Full-Text Articles in Chemistry
N- And C-Terminal Domains In Human Holocarboxylase Synthetase Participate In Substrate Recognition, Yousef I. Hassan, Hideaki Moriyama, Lars J. Olsen, Xin Bi, Janos Zempleni
N- And C-Terminal Domains In Human Holocarboxylase Synthetase Participate In Substrate Recognition, Yousef I. Hassan, Hideaki Moriyama, Lars J. Olsen, Xin Bi, Janos Zempleni
Hideaki Moriyama Publications
Holocarboxylase synthetase (HCS) catalyzes the binding of the vitamin biotin to carboxylases and histones. Carboxylases mediate essential steps in macronutrient metabolism. For example, propionyl- CoA carboxylase (PCC) catalyzes the carboxylation of propionyl-CoA in the metabolism of oddchain fatty acids. HCS comprises four putative domains, i.e., the N-terminus, the biotin transfer/ATP binding domain, a putative linker domain, and the C-terminus. Both N- and C-termini are essential for biotinylation of carboxylases by HCS, but the exact functions of these two domains in enzyme catalysis are unknown. Here we tested the hypothesis that N- and C-termini play roles in substrate recognition by HCS. …
N- And C-Terminal Domains In Human Holocarboxylase Synthetase Participate In Substrate Recognition, Yousef I. Hassan, Hideaki Moriyama, Lars J. Olsen, Xin Bi, Janos Zempleni
N- And C-Terminal Domains In Human Holocarboxylase Synthetase Participate In Substrate Recognition, Yousef I. Hassan, Hideaki Moriyama, Lars J. Olsen, Xin Bi, Janos Zempleni
Hideaki Moriyama Publications
Holocarboxylase synthetase (HCS) catalyzes the binding of the vitamin biotin to carboxylases and histones. Carboxylases mediate essential steps in macronutrient metabolism. For example, propionyl- CoA carboxylase (PCC) catalyzes the carboxylation of propionyl-CoA in the metabolism of oddchain fatty acids. HCS comprises four putative domains, i.e., the N-terminus, the biotin transfer/ATP binding domain, a putative linker domain, and the C-terminus. Both N- and C-termini are essential for biotinylation of carboxylases by HCS, but the exact functions of these two domains in enzyme catalysis are unknown. Here we tested the hypothesis that N- and C-termini play roles in substrate recognition by HCS. …
Identification Of Guanylate Cyclases And Related Signaling Proteins In Sperm Tail From Sea Stars By Mass Spectrometry, Mia Nakachi, Midori Matsumoto, Philip M. Terry, Ronald L. Cerny, Hideaki Moriyama
Identification Of Guanylate Cyclases And Related Signaling Proteins In Sperm Tail From Sea Stars By Mass Spectrometry, Mia Nakachi, Midori Matsumoto, Philip M. Terry, Ronald L. Cerny, Hideaki Moriyama
Hideaki Moriyama Publications
Marine invertebrates employ external fertilization to take the advantages of sexual reproduction as one of excellent survival strategies. To prevent mismatching, successful fertilization can be made only after going though strictly defined steps in the fertilization. In sea stars, the fertilization process starts with the chemotaxis of sperm followed by hyperactivation of sperm upon arriving onto the egg coat, and then sperm penetrate to the egg coat before achieving the fusion. To investigate whether the initiation of chemotaxis and the following signaling has species specificity, we conducted comparative studies in the protein level among sea stars, Asterias amurensis, A. forbesi …
Mechanisms Of Hemoglobin Adaptation To High Altitude Hypoxia, Jay F. Storz, Hideaki Moriyama
Mechanisms Of Hemoglobin Adaptation To High Altitude Hypoxia, Jay F. Storz, Hideaki Moriyama
Hideaki Moriyama Publications
Evidence from a number of vertebrate taxa suggests that modifications of hemoglobin (Hb) function may often play a key role in mediating an adaptive response to high altitude hypoxia. The respiratory functions of Hb are a product of the protein’s intrinsic O2-binding affinity and its interactions with allosteric effectors such as protons, chloride ions, CO2, and organic phosphates. Here we review several case studies involving high altitude vertebrates where it has been possible to identify specific mechanisms of Hb adaptation to hypoxia. In addition to comparative studies of Hbs from diverse animal species, functional studies of …
Conserved Sequences Of Sperm-Activating Peptide And Its Receptor Throughout Evolution, Despite Speciation In The Sea Star Asterias Amurensis And Closely Related Species, Mia Nakachi, Motonori Hoshi, Midori Matsumoto, Hideaki Moriyama
Conserved Sequences Of Sperm-Activating Peptide And Its Receptor Throughout Evolution, Despite Speciation In The Sea Star Asterias Amurensis And Closely Related Species, Mia Nakachi, Motonori Hoshi, Midori Matsumoto, Hideaki Moriyama
Hideaki Moriyama Publications
The asteroidal sperm-activating peptides (asterosaps) from the egg jelly bind to their sperm receptor, a membrane-bound guanylate cyclase, on the tail to activate sperm in sea stars. Asterosaps are produced as single peptides and then cleaved into shorter peptides. Sperm activation is followed by the acrosome reaction, which is subfamily specific. In order to investigate the molecular details of the asterosap-receptor interaction, corresponding cDNAs have been cloned, sequenced and analysed from the Asteriinae subfamily including Asterias amurensis, A. rubens, A. jorbesi and Aphelasterias japonica, as well as Distolasterias nipon from the Coscinasteriinae subfamily. Averages of 29% and 86% identity …
Mechanisms Of Hemoglobin Adaptation To High Altitude Hypoxia, Jay F. Storz, Hideaki Moriyama
Mechanisms Of Hemoglobin Adaptation To High Altitude Hypoxia, Jay F. Storz, Hideaki Moriyama
Hideaki Moriyama Publications
Evidence from a number of vertebrate taxa suggests that modifications of hemoglobin (Hb) function may often play a key role in mediating an adaptive response to high altitude hypoxia. The respiratory functions of Hb are a product of the protein’s intrinsic O2-binding affinity and its interactions with allosteric effectors such as protons, chloride ions, CO2, and organic phosphates. Here we review several case studies involving high altitude vertebrates where it has been possible to identify specific mechanisms of Hb adaptation to hypoxia. In addition to comparative studies of Hbs from diverse animal species, functional studies of …
Supporting Information For "The Molecular Basis Of High-Altitude Adaptation In Deer Mice", Jay F. Storz, Stephen J. Sabatino, Federico G. Hoffmann, Eben J. Gering, Hideaki Moriyama, Nuno Ferrand, Bruno Monteiro, Michael W. Nachman
Supporting Information For "The Molecular Basis Of High-Altitude Adaptation In Deer Mice", Jay F. Storz, Stephen J. Sabatino, Federico G. Hoffmann, Eben J. Gering, Hideaki Moriyama, Nuno Ferrand, Bruno Monteiro, Michael W. Nachman
Hideaki Moriyama Publications
Figure S1: Variation in Site-Specific Levels of Altitudinal Differentiation across the 5′ α- Globin Gene of P. maniculatus
Figure S2: Relationship between Pairwise Linkage Disequilibrium and Distance in bp
Genbank Accession Numbers
Table S1: Amino Acid Variation in the α-Globin Genes of High- and Low-Altitude Deer Mice: Amino acid replacement polymorphisms in deer mice where the derived variant is present at a frequency of >0.100 in the high-altitude sample.
Table S2: Additional Information on Sequenced Loci: Primer sequences for nuclear loci in P. maniculatus.
The Molecular Basis Of High-Altitude Adaptation In Deer Mice, Jay F. Storz, Stephen J. Sabatino, Federico G. Hoffmann, Eben J. Gering, Hideaki Moriyama, Nuno Ferrand, Bruno Monteiro, Michael W. Nachman
The Molecular Basis Of High-Altitude Adaptation In Deer Mice, Jay F. Storz, Stephen J. Sabatino, Federico G. Hoffmann, Eben J. Gering, Hideaki Moriyama, Nuno Ferrand, Bruno Monteiro, Michael W. Nachman
Hideaki Moriyama Publications
Elucidating genetic mechanisms of adaptation is a goal of central importance in evolutionary biology, yet few empirical studies have succeeded in documenting causal links between molecular variation and organismal fitness in natural populations. Here we report a population genetic analysis of a two-locus a-globin polymorphism that underlies physiological adaptation to high-altitude hypoxia in natural populations of deer mice, Peromyscus maniculatus. This system provides a rare opportunity to examine the molecular underpinnings of fitness-related variation in protein function that can be related to a well-defined selection pressure. We surveyed DNA sequence variation in the duplicated α -globin genes of P. maniculatus …
Apparatus And Method For Growing Crystal, And Apparatus And Method For Analyzing Crystal: United States Patent No. 7,156,917 B2, Hideaki Moriyama, Norio Sugi, Kazunori Kawasaki, Shoji Muramatsu
Apparatus And Method For Growing Crystal, And Apparatus And Method For Analyzing Crystal: United States Patent No. 7,156,917 B2, Hideaki Moriyama, Norio Sugi, Kazunori Kawasaki, Shoji Muramatsu
Hideaki Moriyama Publications
An apparatus for growing a biological macromolecular crystal by vaporizing biological macromolecular solution into an oversaturated state. The apparatus includes a first sealed room that receives first crystallizing agent solution, and a communicating tube that communicates with the first sealed room and has a small sectional area for suppressing convection of air. A plurality of droplets of solution dissolving a biological macromolecule and a crystallizing agent therein are held in the communicating tube with the plurality of droplets being separated from each other.
Acrosome Reaction Is Subfamily Specific In Sea Star Fertilization, Mia Nakachi, Hideaki Moriyama, Motonori Hoshi, Midori Matsumoto
Acrosome Reaction Is Subfamily Specific In Sea Star Fertilization, Mia Nakachi, Hideaki Moriyama, Motonori Hoshi, Midori Matsumoto
Hideaki Moriyama Publications
In the fertilization process of sea stars, sperm is activated to go through the acrosome reaction before cell fusion. We focused on induction of the acrosome reaction as a key process in fertilization. Six species of sea stars were used in this study: Asterias amurensis, Asterias rubens, Asterias forbesi, Aphelasterias japonica, Distolasterias nipon, and Asterina pectinifera. Acrosome reaction assays indicate that the acrosome reaction can be induced across species within Asteriinae subfamily. However, cross-fertilization assays indicate that sea stars have species specificity in fertilization. Therefore, steps after the acrosome reaction are responsible for the …
The Importance Of The Strictly Conserved, C-Terminal Glycine Residue In Phosphoenolpyruvate Carboxylase For Overall Catalysis: Mutagenesis And Truncation Of Gly-961 In The Sorghum C4 Leaf Isoform, Wenxin Xu, Shaheen Ahmed, Hideaki Moriyama, Raymond Chollet
The Importance Of The Strictly Conserved, C-Terminal Glycine Residue In Phosphoenolpyruvate Carboxylase For Overall Catalysis: Mutagenesis And Truncation Of Gly-961 In The Sorghum C4 Leaf Isoform, Wenxin Xu, Shaheen Ahmed, Hideaki Moriyama, Raymond Chollet
Hideaki Moriyama Publications
Phosphoenolpyruvate carboxylase (PEPC) is a “multifaceted,” allosteric enzyme involved in C4 acid metabolism in green plants/microalgae and prokaryotes. Before the elucidation of the three-dimensional structures of maize C4 leaf and Escherichia coli PEPC, our truncation analysis of the sorghum C4 homologue revealed important roles for the enzyme’s C-terminal α-helix and its appended QNTG961 tetrapeptide in polypeptide stability and overall catalysis, respectively. Collectively, these functional and structural observations implicate the importance of the PEPC C-terminal tetrapeptide for both catalysis and negative allosteric regulation. We have now more finely dissected this element of PEPC structure-function by modification of the absolutely conserved …
Chlorella Virus-Encoded Deoxyuridine Triphosphatases Exhibit Different Temperature Optima, Yuanzheng Zhang, Hideaki Moriyama, Kohei Homma, James L. Van Etten
Chlorella Virus-Encoded Deoxyuridine Triphosphatases Exhibit Different Temperature Optima, Yuanzheng Zhang, Hideaki Moriyama, Kohei Homma, James L. Van Etten
Hideaki Moriyama Publications
A putative deoxyuridine triphosphatase (dUTPase) gene from chlorella virus PBCV-1 was cloned, and the recombinant protein was expressed in Escherichia coli. The recombinant protein has dUTPase activity and requires Mg2+ for optimal activity, while it retains some activity in the presence of other divalent cations. Kinetic studies of the enzyme revealed a Km of 11.7 μ M, a turnover kcat of 6.8 s-1, and a catalytic efficiency of kcat/Km = 5.8 x 105 M-1 s-1. dUTPase genes were cloned and expressed from two other chlorella viruses …