scholarly journals Nucleotide sequence of c-H-ras-1 gene from B6C3F1 mice.

1996 ◽  
Vol 43 (3) ◽  
pp. 575-578 ◽  
Author(s):  
B Przybojewska ◽  
G Płucienniczak
Keyword(s):  
Amino Acids ◽  
Nucleotide Sequence ◽  
Protein Sequence ◽  
Human Gene ◽  
Ras Gene ◽  
Nucleotide Level ◽  
B6c3f1 Mouse ◽  
B6c3f1 Mice ◽  
High Degree

The c-H-ras-1 gene of an B6C3F1 mouse was isolated and nucleotide sequence determined. Our study has revealed that this c-H-ras-1 gene consists of four exons, separated by three introns ranging in size from 150 to 649 bp. The coding parts of the sequence of mouse c-H-ras-1 gene show no important differences as compared with those of the rat, hamster and human gene. More numerous changes were found in introns. The identity of mouse c-H-ras-1 gene with rat, hamster and human ones at the nucleotide level is 86.40%, 80.04% and 67.87%, respectively. Comparison of amino acids in protein sequence of c-H-ras gene of mouse, rat, hamster and human points to high degree of conservation of the gene.

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.

A protein sequence study of the dicotyledons and its relevance to the evolution of the legumes and nitrogen fixation

1990 ◽  
Vol 3 (1) ◽  
pp. 91 ◽  
Author(s):  
PG Martin ◽  
JM Dowd
Keyword(s):  
Amino Acids ◽  
Nitrogen Fixation ◽  
Protein Sequence ◽  
Maximum Parsimony ◽  
Small Subunit ◽  
Bisphosphate Carboxylase ◽  
Ancestral Sequences ◽  
High Degree ◽  
Working Hypotheses ◽  
Sequence Study

The data were the N-terminal 40 amino acids of the small subunit of ribulose-1,5-bisphosphate carboxylase (Rubisco-SSU) from 310 dicotyledons covering about half the families and most orders. The strategy used to build an overall phylogenetic tree is described; a maximum parsimony program, reliable for up to 17 taxa, has been used. The first step was to use four modern phylogenies to divide 101 of the families into 25 Groups of uneven size leaving 20 families with controversial affinities. Ancestral sequences were derived for each group and these were built into an overall tree in five stages that included testing the reality of the original Groups and re-defining a third of them to include most of the families of controversial affinities. The high degree of taxonomically 'correct' clustering of taxa into families suggested reliability at that level, but reliability probably diminished at higher levels that are separated by shorter distances. The results should be regarded as working hypotheses for future investigations, not as firm conclusions. Evidence is presented that, of the three leguminous families, Mimosaceae and Papilionaceae are closest and that Caesalpiniaceae is very close to Rosaceae. Families in which nitrogen fixation is known appear to associate in three clusters comprising one, three and eight families.

scholarly journals The pentafunctional arom enzyme of Saccharomyces cerevisiae is a mosaic of monofunctional domains

1987 ◽  
Vol 246 (2) ◽  
pp. 375-386 ◽  
Author(s):  
K Duncan ◽  
R M Edwards ◽  
J R Coggins
Keyword(s):  
Escherichia Coli ◽  
Saccharomyces Cerevisiae ◽  
Amino Acids ◽  
Nucleotide Sequence ◽  
Protein Sequence ◽  
Polypeptide Chain ◽  
Functional Domains ◽  
E Coli ◽  
Multifunctional Enzyme ◽  
Functional Regions

The nucleotide sequence of the Saccharomyces cerevisiae ARO1 gene which encodes the arom multifunctional enzyme has been determined. The protein sequence deduced for the pentafunctional arom polypeptide is 1588 amino acids in length and has a calculated Mr of 174555. Functional regions within the polypeptide chain have been identified by comparison with the sequences of the five monofunctional Escherichia coli enzymes whose activities correspond with those of the arom multifunctional enzyme. The observed homologies demonstrate that the arom polypeptide is a mosaic of functional domains and are consistent with the hypothesis that the ARO1 gene evolved by the linking of ancestral E. coli-like genes.

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.

Nucleotide sequence of a cDNA coding for mitochondrial fumarase from human liver

1986 ◽  
Vol 6 (10) ◽  
pp. 921-929 ◽  
Author(s):  
B. Therese Kinsella ◽  
Shawn Doonan
Keyword(s):  
Escherichia Coli ◽  
Amino Acids ◽  
Nucleotide Sequence ◽  
Human Liver ◽  
Chain Termination ◽  
Open Reading Frame ◽  
Antigenic Determinants ◽  
Reading Frame ◽  
E Coli ◽  
High Degree

The nucleotide sequence of a 1.46 kb cDNA, selected from a human liver library by the expression of fumarase antigenic determinants, was determined using the dideoxy chain termination method. The cDNA contained an open reading frame extending from the extreme 5′-base and coding for a protein with 468 amino acids. This protein, with the exception of an N-terminal methionine, was identified as mitochondrial fumarase. The protein showed a high degree of identity of structure with the fumarase from Bacillus subtilis (56.6 %) and a fumarase from Escherichia coli (product of the fumC gene, 59.3 %), and a lower degree of identity with the aspartase of E. coli (37.2 %).

scholarly journals NCBI Taxonomy: a comprehensive update on curation, resources and tools

Database ◽  
2020 ◽  
Vol 2020 ◽  
Author(s):  
Conrad L Schoch ◽  
Stacy Ciufo ◽  
Mikhail Domrachev ◽  
Carol L Hotton ◽  
Sivakumar Kannan ◽  
...  
Keyword(s):  
Nucleotide Sequence ◽  
Protein Sequence ◽  
Ncbi Taxonomy ◽  
Sequence Database ◽  
External Resources ◽  
International Nucleotide Sequence Database ◽  
Sql Database ◽  
Data Elements ◽  
Taxonomic Groups ◽  
Nucleotide Sequence Database

Abstract The National Center for Biotechnology Information (NCBI) Taxonomy includes organism names and classifications for every sequence in the nucleotide and protein sequence databases of the International Nucleotide Sequence Database Collaboration. Since the last review of this resource in 2012, it has undergone several improvements. Most notable is the shift from a single SQL database to a series of linked databases tied to a framework of data called NameBank. This means that relations among data elements can be adjusted in more detail, resulting in expanded annotation of synonyms, the ability to flag names with specific nomenclatural properties, enhanced tracking of publications tied to names and improved annotation of scientific authorities and types. Additionally, practices utilized by NCBI Taxonomy curators specific to major taxonomic groups are described, terms peculiar to NCBI Taxonomy are explained, external resources are acknowledged and updates to tools and other resources are documented. Database URL: https://www.ncbi.nlm.nih.gov/taxonomy

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.

Nucleotide sequence of a ras gene from the basidiomycete Coprinus cinereus

Gene ◽  
1993 ◽  
Vol 125 (2) ◽  
pp. 233-234 ◽  
Author(s):  
Osamu Ishibashi ◽  
Kazuo Shishido
Keyword(s):  
Nucleotide Sequence ◽  
Coprinus Cinereus ◽  
Ras Gene
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