Cloning and molecular analysis of the human citrate synthase gene

Genome ◽  
1998 ◽  
Vol 41 (5) ◽  
pp. 733-738 ◽  
Author(s):  
Michael J Goldenthal ◽  
Jose Marin-Garcia ◽  
Radha Ananthakrishnan
Keyword(s):  
Amino Acids ◽  
Nucleotide Sequence ◽  
Human Heart ◽  
Citrate Synthase ◽  
Krebs Cycle ◽  
Chromosome 12 ◽  
Primary Sequence ◽  
Key Words Human ◽  
Human Genomic ◽  
Sequence Encoding

The nucleotide sequence encoding the citrate synthase (CS) gene was determined from the sequencing of the CS cDNA isolated from a human heart cDNA library. The primary sequence of CS deduced from its nucleotide sequence reveals a highly conserved, albeit slightly larger, protein of 466 amino acids, with 95% homology to its pig homologue. The data also indicate that the human genomic CS gene contains no introns, and confirms the location of the human CS gene on chromosome 12.Key words: human, citrate synthase, Krebs' cycle.

Structure and expression of a tandem gene pair in Leishmania donovani that encodes a protein structurally homologous to eucaryotic cation-transporting ATPases

1987 ◽  
Vol 7 (11) ◽  
pp. 3937-3946
Author(s):  
J C Meade ◽  
J Shaw ◽  
S Lemaster ◽  
G Gallagher ◽  
J R Stringer
Keyword(s):  
Amino Acids ◽  
Nucleotide Sequence ◽  
Tandem Repeat ◽  
Base Pair ◽  
Leishmania Donovani ◽  
Oligonucleotide Probe ◽  
Open Reading Frame ◽  
Reading Frame ◽  
Atpase Gene ◽  
Sequence Encoding

An oligonucleotide probe was used to clone a cation-transporting ATPase gene from the genome of Leishmania donovani. The nucleotide sequence of the gene contained a 2,922-base-pair open reading frame that was predicted to encode a 107,406-dalton protein composed of 974 amino acids. The predicted L. donovani protein contained all the structural and functional domains expected to be present in a cation-transporting ATPase of the aspartyl phosphate class. The nucleotide sequence encoding the ATPase gene was duplicated in tandem in the parasite genome. Partial sequenation of the second member of the tandem repeat, which lay 2 kilobase pairs downstream of the ATPase gene, indicated that it was either identical to the first gene or very closely related to it. RNA homologous to either the ATPase gene or its adjacent relative was 5 kilobases in size and was approximately equally abundant in both promastigote and amastigote forms of the organism.

scholarly journals Structure and expression of a tandem gene pair in Leishmania donovani that encodes a protein structurally homologous to eucaryotic cation-transporting ATPases.

1987 ◽  
Vol 7 (11) ◽  
pp. 3937-3946 ◽  
Author(s):  
J C Meade ◽  
J Shaw ◽  
S Lemaster ◽  
G Gallagher ◽  
J R Stringer
Keyword(s):  
Amino Acids ◽  
Nucleotide Sequence ◽  
Tandem Repeat ◽  
Base Pair ◽  
Leishmania Donovani ◽  
Oligonucleotide Probe ◽  
Open Reading Frame ◽  
Reading Frame ◽  
Atpase Gene ◽  
Sequence Encoding

An oligonucleotide probe was used to clone a cation-transporting ATPase gene from the genome of Leishmania donovani. The nucleotide sequence of the gene contained a 2,922-base-pair open reading frame that was predicted to encode a 107,406-dalton protein composed of 974 amino acids. The predicted L. donovani protein contained all the structural and functional domains expected to be present in a cation-transporting ATPase of the aspartyl phosphate class. The nucleotide sequence encoding the ATPase gene was duplicated in tandem in the parasite genome. Partial sequenation of the second member of the tandem repeat, which lay 2 kilobase pairs downstream of the ATPase gene, indicated that it was either identical to the first gene or very closely related to it. RNA homologous to either the ATPase gene or its adjacent relative was 5 kilobases in size and was approximately equally abundant in both promastigote and amastigote forms of the organism.

scholarly journals Cloning of a Novel Gene Encoding β-1,3-Xylosidase from a Marine Bacterium, Vibrio sp. Strain XY-214, and Characterization of the Gene Product

2007 ◽  
Vol 74 (1) ◽  
pp. 305-308 ◽  
Author(s):  
Yoshiaki Umemoto ◽  
Ryosuke Onishi ◽  
Toshiyoshi Araki
Keyword(s):  
Escherichia Coli ◽  
Amino Acids ◽  
Molecular Weight ◽  
Nucleotide Sequence ◽  
Gene Product ◽  
Marine Bacterium ◽  
Gene Encoding ◽  
Novel Gene ◽  
Sequence Encoding

ABSTRACT The β-1,3-xylosidase gene (xloA) of Vibrio sp. strain XY-214 was cloned and expressed in Escherichia coli. The xloA gene consisted of a 1,608-bp nucleotide sequence encoding a protein of 535 amino acids with a predicted molecular weight of 60,835. The recombinant β-1,3-xylosidase hydrolyzed β-1,3-xylooligosaccharides to d-xylose as a final product.

scholarly journals Two Pathways for Glutamate Biosynthesis in the Syntrophic Bacterium Syntrophus aciditrophicus

2015 ◽  
Vol 81 (24) ◽  
pp. 8434-8444 ◽  
Author(s):  
Marie Kim ◽  
Huynh M. Le ◽  
Xiulan Xie ◽  
Xueyang Feng ◽  
Yinjie J. Tang ◽  
...  
Keyword(s):  
Amino Acids ◽  
Citrate Synthase ◽  
Carbon Sources ◽  
Krebs Cycle ◽  
Content Type ◽  
Cell Extracts ◽  
Cyclohexane Carboxylate ◽  
Glutamate Synthesis ◽  
Glutamate Biosynthesis ◽  
Syntrophus Aciditrophicus

ABSTRACTThe anaerobic metabolism of crotonate, benzoate, and cyclohexane carboxylate bySyntrophus aciditrophicusgrown syntrophically withMethanospirillum hungateiprovides a model to study syntrophic cooperation. Recent studies revealed thatS. aciditrophicuscontainsRe-citrate synthase but lacks the commonSi-citrate synthase. To establish whether theRe-citrate synthase is involved in glutamate synthesis via the oxidative branch of the Krebs cycle, we have used [1-13C]acetate and [1-14C]acetate as well as [13C]bicarbonate as additional carbon sources during axenic growth ofS. aciditrophicuson crotonate. Our analyses showed that labeled carbons were detected in at least 14 amino acids, indicating the global utilization of acetate and bicarbonate. The labeling patterns of alanine and aspartate verified that pyruvate and oxaloacetate were synthesized by consecutive carboxylations of acetyl coenzyme A (acetyl-CoA). The isotopomer profile and13C nuclear magnetic resonance (NMR) spectroscopy of the obtained [13C]glutamate, as well as decarboxylation of [14C]glutamate, revealed that this amino acid was synthesized by two pathways. Unexpectedly, only the minor route usedRe-citrate synthase (30 to 40%), whereas the majority of glutamate was synthesized via the reductive carboxylation of succinate. This symmetrical intermediate could have been formed from two acetates via hydration of crotonyl-CoA to 4-hydroxybutyryl-CoA. 4-Hydroxybutyrate was detected in the medium ofS. aciditrophicuswhen grown on crotonate, but an active hydratase could not be measured in cell extracts, and the annotated 4-hydroxybutyryl-CoA dehydratase (SYN_02445) lacks key amino acids needed to catalyze the hydration of crotonyl-CoA. BesidesClostridium kluyveri, this study reveals the second example of a microbial species to employ two pathways for glutamate synthesis.

scholarly journals Nucleotide sequence of the two rat cellular rasH genes.

1986 ◽  
Vol 6 (5) ◽  
pp. 1706-1710 ◽  
Author(s):  
M Ruta ◽  
R Wolford ◽  
R Dhar ◽  
D Defeo-Jones ◽  
R W Ellis ◽  
...  
Keyword(s):  
Amino Acids ◽  
Nucleotide Sequence ◽  
Coding Region ◽  
3T3 Cells ◽  
Ras Gene ◽  
P21 Protein ◽  
Murine Sarcoma Virus ◽  
Sarcoma Virus ◽  
Nih 3T3 ◽  
Murine Sarcoma

We present the nucleotide sequence of the coding region of the rat c-rasH-1 gene and a partial sequence analysis of the rat c-rasH-2 gene. By comparing these sequences with the Harvey murine sarcoma virus ras gene, we predict that the p21 protein encoded by the Harvey virus differs from the cellular c-rasH-1-encoded p21 at only two amino acids; those at positions 12 and 59. Alterations at each of these positions may play a role in activating the viral p21 protein. The c-rasH-2 gene is likely to be a nonfunctional pseudogene because it lacks introns, cannot be activated to transform NIH 3T3 cells, and differs in sequence from both c-rasH-1 and v-rasH at several base pair positions.

scholarly journals Cloning, Nucleotide Sequence, and Expression of the Gene Encoding the Bacteriocin Boticin B from Clostridium botulinum Strain 213B

2000 ◽  
Vol 66 (12) ◽  
pp. 5480-5483 ◽  
Author(s):  
Sean S. Dineen ◽  
Marite Bradshaw ◽  
Eric A. Johnson
Keyword(s):  
Amino Acids ◽  
Nucleotide Sequence ◽  
Clostridium Botulinum ◽  
Shuttle Vector ◽  
Open Reading Frame ◽  
Gene Encoding ◽  
Reading Frame ◽  
Heat Stable ◽  
Group I

ABSTRACT Boticin B is a heat-stable bacteriocin produced byClostridium botulinum strain 213B that has inhibitory activity against various strains of C. botulinum and related clostridia. The gene encoding the bacteriocin was localized to a 3.0-kb HindIII fragment of an 18.8-kb plasmid, cloned, and sequenced. DNA sequencing revealed the boticin B structural gene,btcB, to be an open reading frame encoding 50 amino acids. A C. botulinum strain 62A transconjugant containing theHindIII fragment inserted into a clostridial shuttle vector expressed boticin B, although at much lower levels than those observed in C. botulinum 213B. To our knowledge, this is the first demonstration and characterization of a bacteriocin from toxigenic group I C. botulinum.

scholarly journals Nucleotide sequence of the promoter region of the citrate synthase gene (gltA) of Escherichia coli

FEBS Letters ◽  
1983 ◽  
Vol 156 (2) ◽  
pp. 366-370 ◽  
Author(s):  
Elizabeth P. Hull ◽  
Margaret E. Spencer ◽  
David Wood ◽  
John R. Guest
Keyword(s):  
Escherichia Coli ◽  
Nucleotide Sequence ◽  
Promoter Region ◽  
Citrate Synthase

scholarly journals The Complete Nucleotide Sequence and Biotype Variability of Papaya leaf distortion mosaic virus

2005 ◽  
Vol 95 (2) ◽  
pp. 128-135 ◽  
Author(s):  
Tetsuo Maoka ◽  
Tatsuji Hataya
Keyword(s):  
Amino Acids ◽  
Nucleotide Sequence ◽  
Mosaic Virus ◽  
Complete Nucleotide Sequence ◽  
Distinct Species ◽  
Cleavage Sites ◽  
Reading Frame ◽  
The Family ◽  
Evolutionary Event ◽  
Leaf Distortion

The complete nucleotide sequence of the genome of Papaya leaf distortion mosaic virus (PLDMV) was determined. The viral RNA genome of strain LDM (leaf distortion mosaic) comprised 10,153 nucleotides, excluding the poly(A) tail, and contained one long open reading frame encoding a polyprotein of 3,269 amino acids (molecular weight 373,347). The polyprotein contained nine putative proteolytic cleavage sites and some motifs conserved in other potyviral polyproteins with 44 to 50% identities, indicating that PLDMV is a distinct species in the genus Potyvirus. Like the W biotype of Papaya ringspot virus (PRSV), the non-papaya-infecting biotype of PLDMV (PLDMV-C) was found in plants of the family Cucurbitaceae. The coat protein (CP) sequence of PLDMV-C in naturally infected-Trichosanthes bracteata was compared with those of three strains of the P biotype (PLDMV-P), LDM and two additional strains M (mosaic) and YM (yellow mosaic), which are biologically different from each other. The CP sequences of three strains of PLDMV-P share high identities of 95 to 97%, while they share lower identities of 88 to 89% with that of PLDMV-C. Significant changes in hydrophobicity and a deletion of two amino acids at the N-terminal region of the CP of PLDMV-C were observed. The finding of two biotypes of PLDMV implies the possibility that the papaya-infecting biotype evolved from the cucurbitaceae-infecting potyvirus, as has been previously suggested for PRSV. In addition, a similar evolutionary event acquiring infectivity to papaya may arise frequently in viruses in the family Cucurbitaceae.

scholarly journals Biophysics : Aspects of Amino Acids Sequence in Proteins and Nucleotide Sequence in Nucleic Acids

2013 ◽  
Vol 4 ◽  
pp. 65-74
Author(s):  
Khadka Bahadur Chhetri
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Nucleotide Sequence ◽  
Amino Acid Sequence ◽  
Nucleic Acids ◽  
Polypeptide Chain ◽  
Antibody Complex ◽  
Antigen Antibody

Protein is the polypeptide chain of amino-acid sequence. Proteins of all species, from bacteria to humans, are made up from the same set of 20 standard amino acids. In order to carry out their function they must take a particular shape which is known as fold. All the enzymes hormones and antibodies are also proteins. To treat certain toxic-microorganism or invader we need certain antigen-antibody complex in the organisms. Just as amino-acid sequence forms the proteins, the polynucleotide sequence forms the nucleic acids. The gene is a part of DNA macromolecule responsible for the synthesis of protein chains. There are 20 amino-acids responsible for the formation of protein and 4 nucleotides responsible for the formation of DNA (RNA). Therefore, we can say that protein text is written in 20-letter and the DNA (RNA) text is written in 4-letter language. The information contained in genes in DNA is transferred to mRNA during transcription.The Himalayan Physics Vol. 4, No. 4, 2013 Page: 65-74 Uploaded date: 12/23/2013 

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