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Katsuji Hori - One of the best experts on this subject based on the ideXlab platform.
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A developmental biological study of Aldolase gene expression in Xenopus laevis
Cell Research, 2002Co-Authors: Koichiro Shiokawa, Eri Kajita, Hitomi Yatsuki, Hiroshi Hara, Katsuji HoriAbstract:We cloned cDNAs for Xenopus Aldolases A, B and C. These three Aldolase genes are localized on different chromosomes as a single copy gene. In the adult, the Aldolase A gene is expressed extensively in muscle tissues, whereas the Aldolase B gene is expressed strongly in kidney, liver, stomach and intestine, while the Aldolase C gene is expressed in brain, heart and ovary. In oocytes Aldolase A and C mRNAs, but not Aldolase B mRNA, are extensively transcribed. Thus, Aldolase A and C mRNAs, but not B mRNA, occur abundantly in eggs as maternal mRNAs, and strong expression of Aldolase B mRNA is seen only after the late neurula stage. We conclude that Aldolase A and C mRNAs are major Aldolase mRNAs in early stages of Xenopus embryogenesis which proceeds utilizing yolk as the only energy source. Aldolase B mRNA, on the other hand, is expressed only later in development in tissues which are required for dietary fructose metabolism. We also isolated the Xenopus Aldolase C genomic gene (ca. 12 kb) and found that its promoter (ca. 2 kb) contains regions necessary for tissue-specific expression and also a GC rich region which is essential for basal transcriptional activity.
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quantitative expression studies of Aldolase a b and c genes in developing embryos and adult tissues of xenopus laevis
Mechanisms of Development, 2001Co-Authors: Eri Kajita, Hitomi Yatsuki, Katsuji Hori, Kinichiro Miura, Junya Moriwaki, Momoki Hirai, Koichiro ShiokawaAbstract:Abstract We previously cloned cDNAs for all the members (A, B and C) of Xenopus Aldolase gene family, and using in vitro transcribed RNAs as references, performed quantitative studies of the expression of three Aldolase mRNAs in embryos and adult tissues. A Xenopus egg contains ca. 60 pg Aldolase A mRNA and ca. 45 pg Aldolase C mRNA, but contains only ca. 1.5 pg Aldolase B mRNA. The percent composition of three Aldolase mRNAs (A:B:C) changes from 56:1.5:42.5 (fertilized egg) to 54:10:36 (gastrula), to 71:14.5:14.5 (neurula) and to 73:20:7 (tadpole) during development. These results are compatible with the previous results of zymogram analysis that Aldolases A and C are the major Aldolases in early embryos, whose development proceeds depending on yolk as the only energy source. Aldolase B mRNA is expressed only late in development in tissues such as pronephros, liver rudiment and proctodeum which are necessary for the future dietary fructose metabolism, and the expression pattern is consistent to that in adult tissues. We also show that three Aldolase genes are localized on different chromosomes as single copy genes.
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isolation and characterization of xenopus laevis Aldolase b cdna and expression patterns of Aldolase a b and c genes in adult tissues oocytes and embryos of xenopus laevis
Biochimica et Biophysica Acta, 2000Co-Authors: Eri Kajita, Motoaki Wakiyama, Hitomi Yatsuki, Katsuji Hori, Kinichiro Miura, Kiyohisa Mizumoto, Issei Komuro, Takashi Miyata, Koichiro ShiokawaAbstract:Abstract Following previous cloning and expression studies of Xenopus Aldolase C (brain-type) and A (muscle-type) cDNAs, we cloned here two Xenopus Aldolase B (liver-type) cDNAs (XALDB1 and XALDB2, 2447 and 1490 bp, respectively) using two different liver libraries. These cDNAs had very similar ORF with only one conservative amino acid substitution, but 3′-UTR of XALDB1 contained ca. 1 kb of unrelated reiterated sequence probably ligated during library construction as shown by genomic Southern blot analysis. In adult, Aldolase B mRNA (ca. 1.8 kb) was expressed strongly in kidney, liver, stomach, intestine, moderately strongly in skin, and very weakly in all the other tissues including muscles and brain, which strongly express Aldolase A and C mRNAs, respectively. In oocytes and early embryos, Aldolase A and C mRNAs occurred abundantly as maternal mRNAs, but Aldolase B mRNA occurred only at a residual level, and its strong expression started only after the late neurula stage, mainly in liver rudiment, pronephros, epidermis and proctodeum. Thus, active expression of the gene for Aldolase B, involved in dietary fructose metabolism, starts only later during development (but before the feeding stage), albeit genes for Aldolases A and C, involved in glycolysis, are expressed abundantly from early stages of embryogenesis, during which embryos develop depending on yolk as the only energy source.
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Role of isozyme group-specific sequence 4 in the isozyme-specific properties of human Aldolase C
Comparative biochemistry and physiology. Part B Biochemistry & molecular biology, 1998Co-Authors: Takahiro Kusakabe, Kiyohisa Motoki, Yasushi Sugimoto, Katsuji HoriAbstract:Abstract To assess which regions of the Aldolase C molecule are required for exhibiting isozyme-specific kinetic properties, we have constructed nine chimeric enzymes of human Aldolases A and C. Kinetic studies of these chimeric enzymes revealed that Aldolase C absolutely required its own isozyme group-specific sequences (IGS), particularly IGS-4, for exhibiting the characteristics of Aldolase C which differ significantly from those of isozymes A and B (Kusakabe T, Motoki K, Hori K. Human Aldolase C: characterization of the recombinant enzyme expressed in Escherichia coli . J Biochem (Tokyo) 1994;115:1172–7). Whereas human Aldolases A and B required their own isozyme group-specific sequences-1 and -4 (IGS-1 and -4) as the main determinants of isozyme-specific kinetic properties (Motoki K, Kitajima Y, Hori K. Isozyme-specific modules on human Aldolase A molecule. J Biol Chem 1993;268:1677–83; Kusakabe T, Motoki K, Sugimoto Y, Takasaki Y, Hori K. Human Aldolase B: liver-specific properties of the isoenzyme depend on type B isozyme group-specific sequence. Prot. Eng. 1994;7:1387–93), the present studies indicate that the IGS-1 is principally substitutable between Aldolases A and C. The kinetic data also suggests that the connector-2 (amino acid residues 243–306) may modulate the interaction of IGS units with the α / β barrel of the Aldolase molecule.
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Mode of Interactions of Human Aldolase Isozymes with Cytoskeletons
Archives of Biochemistry and Biophysics, 1997Co-Authors: Takahiro Kusakabe, Kiyohisa Motoki, Katsuji HoriAbstract:Three isoforms of fructose-1,6-bisphosphate Aldolase were found to bind specifically to the actin-containing filament of the cytoskeleton and to show tissue-specific binding patterns. Aldolase A (muscle type) bound more tightly to the skeletal muscle cytoskeleton among the three isozymes, while Aldolase B (liver type) preferred the liver cytoskeleton to those of other tissues. The specific binding of Aldolase A to the skeletal muscle cytoskeleton was inhibited strongly by the substrates fructose 1,6-bisphosphate and fructose 1-phosphate. Several mutant Aldolases A were examined to identify the amino acid residues or regions that play a role in specific binding. Among the mutant Aldolases tested, A-E34D, A-K41N, and A-Y363S exhibited remarkably reduced binding activities. Experiments using FITC-labeled enzymes and Rh-labeled phalloidin disclosed that Aldolase A associated with the cytoskeleton. Specifically, when Aldolase A was incubated with human fibroblast MRC-5 permeabilized with Triton X-100, Aldolase A bound to the actin filaments in the stress fibers within the cell. Aldolase A reversibly inhibited the contraction of MRC-5 cells which usually occurred in the presence of Mg2+-ATP and Ca2+. These results provide direct evidence that Aldolase binds specifically to the actin-containing stress fibers and suggest that Aldolase may regulate cell contraction through its reversible binding to the filaments in the permeabilized MRC-5 fibroblast.
Muhammad Akhtar - One of the best experts on this subject based on the ideXlab platform.
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Pcal_0111, a highly thermostable bifunctional fructose-1,6-bisphosphate Aldolase/phosphatase from Pyrobaculum calidifontis
Extremophiles, 2017Co-Authors: Iram Aziz, Naeem Rashid, Raza Ashraf, Qamar Bashir, Tadayuki Imanaka, Muhammad AkhtarAbstract:Pyrobaculum calidifontis genome harbors an open reading frame Pcal_0111 annotated as fructose bisphosphate Aldolase. Although the gene is annotated as fructose bisphosphate Aldolase, it exhibits a high homology with previously reported fructose-1,6-bisphosphate Aldolase/phosphatase from Thermoproteus neutrophilus . To examine the biochemical properties of Pcal_0111, we have cloned and expressed the gene in Escherichia coli . Purified recombinant Pcal_0111 catalyzed both phosphatase and Aldolase reactions with specific activity values of 4 U and 1.3 U, respectively. These values are highest among the fructose 1,6-bisphosphatases/Aldolases characterized from archaea. The enzyme activity increased linearly with the increase in temperature until 100 °C. Recombinant Pcal_0111 is highly stable with a half-life of 120 min at 100 °C. There was no significant change in the circular dichroism spectra of the protein up to 90 °C. The enzyme activity was not affected by AMP but strongly inhibited by ATP with an IC_50 value of 0.75 mM and mildly by ADP. High thermostability and inhibition by ATP make Pcal_0111 a unique fructose 1,6-bisphosphatase/Aldolase.
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pcal_0111 a highly thermostable bifunctional fructose 1 6 bisphosphate Aldolase phosphatase from pyrobaculum calidifontis
Extremophiles, 2017Co-Authors: Iram Aziz, Naeem Rashid, Raza Ashraf, Qamar Bashir, Tadayuki Imanaka, Muhammad AkhtarAbstract:Pyrobaculum calidifontis genome harbors an open reading frame Pcal_0111 annotated as fructose bisphosphate Aldolase. Although the gene is annotated as fructose bisphosphate Aldolase, it exhibits a high homology with previously reported fructose-1,6-bisphosphate Aldolase/phosphatase from Thermoproteus neutrophilus. To examine the biochemical properties of Pcal_0111, we have cloned and expressed the gene in Escherichia coli. Purified recombinant Pcal_0111 catalyzed both phosphatase and Aldolase reactions with specific activity values of 4 U and 1.3 U, respectively. These values are highest among the fructose 1,6-bisphosphatases/Aldolases characterized from archaea. The enzyme activity increased linearly with the increase in temperature until 100 °C. Recombinant Pcal_0111 is highly stable with a half-life of 120 min at 100 °C. There was no significant change in the circular dichroism spectra of the protein up to 90 °C. The enzyme activity was not affected by AMP but strongly inhibited by ATP with an IC50 value of 0.75 mM and mildly by ADP. High thermostability and inhibition by ATP make Pcal_0111 a unique fructose 1,6-bisphosphatase/Aldolase.
Koichiro Shiokawa - One of the best experts on this subject based on the ideXlab platform.
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A developmental biological study of Aldolase gene expression in Xenopus laevis
Cell Research, 2002Co-Authors: Koichiro Shiokawa, Eri Kajita, Hitomi Yatsuki, Hiroshi Hara, Katsuji HoriAbstract:We cloned cDNAs for Xenopus Aldolases A, B and C. These three Aldolase genes are localized on different chromosomes as a single copy gene. In the adult, the Aldolase A gene is expressed extensively in muscle tissues, whereas the Aldolase B gene is expressed strongly in kidney, liver, stomach and intestine, while the Aldolase C gene is expressed in brain, heart and ovary. In oocytes Aldolase A and C mRNAs, but not Aldolase B mRNA, are extensively transcribed. Thus, Aldolase A and C mRNAs, but not B mRNA, occur abundantly in eggs as maternal mRNAs, and strong expression of Aldolase B mRNA is seen only after the late neurula stage. We conclude that Aldolase A and C mRNAs are major Aldolase mRNAs in early stages of Xenopus embryogenesis which proceeds utilizing yolk as the only energy source. Aldolase B mRNA, on the other hand, is expressed only later in development in tissues which are required for dietary fructose metabolism. We also isolated the Xenopus Aldolase C genomic gene (ca. 12 kb) and found that its promoter (ca. 2 kb) contains regions necessary for tissue-specific expression and also a GC rich region which is essential for basal transcriptional activity.
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quantitative expression studies of Aldolase a b and c genes in developing embryos and adult tissues of xenopus laevis
Mechanisms of Development, 2001Co-Authors: Eri Kajita, Hitomi Yatsuki, Katsuji Hori, Kinichiro Miura, Junya Moriwaki, Momoki Hirai, Koichiro ShiokawaAbstract:Abstract We previously cloned cDNAs for all the members (A, B and C) of Xenopus Aldolase gene family, and using in vitro transcribed RNAs as references, performed quantitative studies of the expression of three Aldolase mRNAs in embryos and adult tissues. A Xenopus egg contains ca. 60 pg Aldolase A mRNA and ca. 45 pg Aldolase C mRNA, but contains only ca. 1.5 pg Aldolase B mRNA. The percent composition of three Aldolase mRNAs (A:B:C) changes from 56:1.5:42.5 (fertilized egg) to 54:10:36 (gastrula), to 71:14.5:14.5 (neurula) and to 73:20:7 (tadpole) during development. These results are compatible with the previous results of zymogram analysis that Aldolases A and C are the major Aldolases in early embryos, whose development proceeds depending on yolk as the only energy source. Aldolase B mRNA is expressed only late in development in tissues such as pronephros, liver rudiment and proctodeum which are necessary for the future dietary fructose metabolism, and the expression pattern is consistent to that in adult tissues. We also show that three Aldolase genes are localized on different chromosomes as single copy genes.
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isolation and characterization of xenopus laevis Aldolase b cdna and expression patterns of Aldolase a b and c genes in adult tissues oocytes and embryos of xenopus laevis
Biochimica et Biophysica Acta, 2000Co-Authors: Eri Kajita, Motoaki Wakiyama, Hitomi Yatsuki, Katsuji Hori, Kinichiro Miura, Kiyohisa Mizumoto, Issei Komuro, Takashi Miyata, Koichiro ShiokawaAbstract:Abstract Following previous cloning and expression studies of Xenopus Aldolase C (brain-type) and A (muscle-type) cDNAs, we cloned here two Xenopus Aldolase B (liver-type) cDNAs (XALDB1 and XALDB2, 2447 and 1490 bp, respectively) using two different liver libraries. These cDNAs had very similar ORF with only one conservative amino acid substitution, but 3′-UTR of XALDB1 contained ca. 1 kb of unrelated reiterated sequence probably ligated during library construction as shown by genomic Southern blot analysis. In adult, Aldolase B mRNA (ca. 1.8 kb) was expressed strongly in kidney, liver, stomach, intestine, moderately strongly in skin, and very weakly in all the other tissues including muscles and brain, which strongly express Aldolase A and C mRNAs, respectively. In oocytes and early embryos, Aldolase A and C mRNAs occurred abundantly as maternal mRNAs, but Aldolase B mRNA occurred only at a residual level, and its strong expression started only after the late neurula stage, mainly in liver rudiment, pronephros, epidermis and proctodeum. Thus, active expression of the gene for Aldolase B, involved in dietary fructose metabolism, starts only later during development (but before the feeding stage), albeit genes for Aldolases A and C, involved in glycolysis, are expressed abundantly from early stages of embryogenesis, during which embryos develop depending on yolk as the only energy source.
Virgil Hélaine - One of the best experts on this subject based on the ideXlab platform.
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2 deoxyribose 5 phosphate Aldolase a remarkably tolerant Aldolase towards nucleophile substrates
Chemical Communications, 2019Co-Authors: Domitille Chambre, Ekaterina Darii, J R Petit, Christine Guerardhelaine, Marielle Lemaire, Marcel Salanoubat, Véronique De Berardinis, Aline Mariage, Virgil HélaineAbstract:We explored a collection of 2-deoxyribose-5-phosphate Aldolases (DERAs) from biodiversity for their nucleophile substrate promiscuity. The DERAs were screened using as nucleophiles propanone, propanal, cyclobutanone, cyclopentanone, dihydroxyacetone, and glycolaldehyde with L-glyceraldehyde-3-phosphate as an electrophile in aldol addition. A DERA from Arthrobacter chlorophenolicus (DERAArthro) efficiently allowed the synthesis of the corresponding aldol adducts in good yields, displaying complementarity in terms of configuration and substrate specificity with fructose-6-phosphate Aldolase, the only previously known Aldolase with a large nucleophile tolerance.
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2 deoxyribose 5 phosphate Aldolase a remarkably tolerant Aldolase towards nucleophile substrates
Chemical Communications, 2019Co-Authors: Domitille Chambre, Ekaterina Darii, J R Petit, Christine Guerardhelaine, Marielle Lemaire, Marcel Salanoubat, Véronique De Berardinis, Aline Mariage, Virgil HélaineAbstract:We explored a collection of 2-deoxyribose-5-phosphate Aldolases (DERAs) from biodiversity for their nucleophile substrate promiscuity. The DERAs were screened using as nucleophiles propanone, propanal, cyclobutanone, cyclopentanone, dihydroxyacetone, and glycolaldehyde with L-glyceraldehyde-3-phosphate as an electrophile in aldol addition. A DERA from Arthrobacter chlorophenolicus (DERAArthro) efficiently allowed the synthesis of the corresponding aldol adducts in good yields, displaying complementarity in terms of configuration and substrate specificity with fructose-6-phosphate Aldolase, the only previously known Aldolase with a large nucleophile tolerance.
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Genome Mining for Innovative Biocatalysts: New Dihydroxyacetone Aldolases for the Chemist’s Toolbox.
ChemCatChem, 2015Co-Authors: Christine Guérard-hélaine, Ekaterina Darii, Virgil Hélaine, Véronique De Berardinis, Aline Mariage, Marine Debacker, Adrien Debard, M. Besnard-gonnet, C. Fernandes, Virginie PellouinAbstract:Stereoselective carboligating enzymes were discovered by a genome mining approach to extend the biocatalysis toolbox. Seven hundred enzymes were selected by sequence comparison from diverse prokaryotic species as representatives of the Aldolase (FSA) family diversity. The aldol reaction tested involved dihydroxyacetone (DHA) and glyceraldehyde-3-phosphate. The hexose-6-phosphate formation was monitored by mass spectrometry. Eighteen enzymes annotated either as transAldolases or Aldolases were found to exhibit a DHA Aldolase activity. Remarkably, six of them proven as Aldolases, and not transAldolases, shared very limited similarities with those currently described. Multiple sequence alignment performed on all enzymes revealed a Tyr in the new DHA Aldolases as found in FSAcoli instead of a Phe usually found in transAldolases. Four of these DHA Aldolases were biochemically characterised in comparison with FSAcoli. In particular, an Aldolase from Listeria monocytogenes exhibited interesting catalytic properties.
Hitomi Yatsuki - One of the best experts on this subject based on the ideXlab platform.
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A developmental biological study of Aldolase gene expression in Xenopus laevis
Cell Research, 2002Co-Authors: Koichiro Shiokawa, Eri Kajita, Hitomi Yatsuki, Hiroshi Hara, Katsuji HoriAbstract:We cloned cDNAs for Xenopus Aldolases A, B and C. These three Aldolase genes are localized on different chromosomes as a single copy gene. In the adult, the Aldolase A gene is expressed extensively in muscle tissues, whereas the Aldolase B gene is expressed strongly in kidney, liver, stomach and intestine, while the Aldolase C gene is expressed in brain, heart and ovary. In oocytes Aldolase A and C mRNAs, but not Aldolase B mRNA, are extensively transcribed. Thus, Aldolase A and C mRNAs, but not B mRNA, occur abundantly in eggs as maternal mRNAs, and strong expression of Aldolase B mRNA is seen only after the late neurula stage. We conclude that Aldolase A and C mRNAs are major Aldolase mRNAs in early stages of Xenopus embryogenesis which proceeds utilizing yolk as the only energy source. Aldolase B mRNA, on the other hand, is expressed only later in development in tissues which are required for dietary fructose metabolism. We also isolated the Xenopus Aldolase C genomic gene (ca. 12 kb) and found that its promoter (ca. 2 kb) contains regions necessary for tissue-specific expression and also a GC rich region which is essential for basal transcriptional activity.
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quantitative expression studies of Aldolase a b and c genes in developing embryos and adult tissues of xenopus laevis
Mechanisms of Development, 2001Co-Authors: Eri Kajita, Hitomi Yatsuki, Katsuji Hori, Kinichiro Miura, Junya Moriwaki, Momoki Hirai, Koichiro ShiokawaAbstract:Abstract We previously cloned cDNAs for all the members (A, B and C) of Xenopus Aldolase gene family, and using in vitro transcribed RNAs as references, performed quantitative studies of the expression of three Aldolase mRNAs in embryos and adult tissues. A Xenopus egg contains ca. 60 pg Aldolase A mRNA and ca. 45 pg Aldolase C mRNA, but contains only ca. 1.5 pg Aldolase B mRNA. The percent composition of three Aldolase mRNAs (A:B:C) changes from 56:1.5:42.5 (fertilized egg) to 54:10:36 (gastrula), to 71:14.5:14.5 (neurula) and to 73:20:7 (tadpole) during development. These results are compatible with the previous results of zymogram analysis that Aldolases A and C are the major Aldolases in early embryos, whose development proceeds depending on yolk as the only energy source. Aldolase B mRNA is expressed only late in development in tissues such as pronephros, liver rudiment and proctodeum which are necessary for the future dietary fructose metabolism, and the expression pattern is consistent to that in adult tissues. We also show that three Aldolase genes are localized on different chromosomes as single copy genes.
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isolation and characterization of xenopus laevis Aldolase b cdna and expression patterns of Aldolase a b and c genes in adult tissues oocytes and embryos of xenopus laevis
Biochimica et Biophysica Acta, 2000Co-Authors: Eri Kajita, Motoaki Wakiyama, Hitomi Yatsuki, Katsuji Hori, Kinichiro Miura, Kiyohisa Mizumoto, Issei Komuro, Takashi Miyata, Koichiro ShiokawaAbstract:Abstract Following previous cloning and expression studies of Xenopus Aldolase C (brain-type) and A (muscle-type) cDNAs, we cloned here two Xenopus Aldolase B (liver-type) cDNAs (XALDB1 and XALDB2, 2447 and 1490 bp, respectively) using two different liver libraries. These cDNAs had very similar ORF with only one conservative amino acid substitution, but 3′-UTR of XALDB1 contained ca. 1 kb of unrelated reiterated sequence probably ligated during library construction as shown by genomic Southern blot analysis. In adult, Aldolase B mRNA (ca. 1.8 kb) was expressed strongly in kidney, liver, stomach, intestine, moderately strongly in skin, and very weakly in all the other tissues including muscles and brain, which strongly express Aldolase A and C mRNAs, respectively. In oocytes and early embryos, Aldolase A and C mRNAs occurred abundantly as maternal mRNAs, but Aldolase B mRNA occurred only at a residual level, and its strong expression started only after the late neurula stage, mainly in liver rudiment, pronephros, epidermis and proctodeum. Thus, active expression of the gene for Aldolase B, involved in dietary fructose metabolism, starts only later during development (but before the feeding stage), albeit genes for Aldolases A and C, involved in glycolysis, are expressed abundantly from early stages of embryogenesis, during which embryos develop depending on yolk as the only energy source.
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structures of cdnas encoding the muscle type and non muscle type isozymes of lamprey fructose bisphosphate Aldolases and the evolution of Aldolase genes
Journal of Biochemistry, 1995Co-Authors: Rong Zhang, Takahiro Kusakabe, Hitomi Yatsuki, Takashi Miyata, Naoyuki Iwabe, Toshio Imai, Mitsutaka Yoshida, Katsuji HoriAbstract:Nearly full-length cDNA clones for muscle-type and non-muscle-type Aldolase mRNAs were cloned from lambda gt10 cDNA libraries constructed from skeletal muscle and liver mRNAs of lamprey (Entosphenus japonicus). The cDNA-M8 has 2,240 bp carrying an open reading frame of 1,089 bp which encodes 362 amino acids without the amino terminal methionine, while the cDNA-L3 is 1,761 bp in length and has an open reading frame of 1,092 bp, which encodes 363 amino acids without the methionine. We designated the cDNA clones M8 and L3 as the muscle-type and non-muscle-type Aldolase cDNAs, respectively. The entire amino acid sequences deduced from cDNA-M8 and -L3 show a high degree of identity to one another (76%) and also to vertebrate Aldolases A (74-76%), B (68-70%), and C (71-76%) and Drosophila melanogaster Aldolases alpha, beta, and gamma (66-67%). Northern blot analyses using the 3'-noncoding sequences of cDNA-M8 and -L3 as hybridization probes indicated that the muscle-type mRNA is expressed mainly in the skeletal muscle, heart muscle, brain, and some other tissues, but probably not in liver, while the non-muscle-type mRNA is expressed mainly in the liver and also in brain and other tissues, except for the heart muscle. Phylogenetic analyses showed that both muscle-type and non-muscle-type Aldolases of lamprey resemble one another and might share a common ancestor with vertebrate Aldolases A and C, but they are not direct ancestors of vertebrate Aldolases.