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Cloning, genomic organization and chromosomal assignment of the mouse p190-B gene.
- Source :
-
Biochimica et biophysica acta [Biochim Biophys Acta] 1998 Nov 26; Vol. 1443 (1-2), pp. 203-10. - Publication Year :
- 1998
-
Abstract
- The p190 family of GTPases consists of at least two different isoforms both containing an N-terminal GTPase and a C-terminal Rho GAP domain. Here we have isolated and characterized genomic and cDNA clones spanning the entire coding region of the mouse p190-B gene. Genomic data were obtained by sequencing plasmid subclones of two overlapping mouse genomic phage clones. Interestingly, a single 3.9 kb exon was found to contain approx. 80% of the coding region of the mouse p190-B protein (amino acid residues 1-1238) including the 5'-untranslated region, the N-terminal GTPase domain and a middle domain of unknown function. Missing from this exon, however, was the C-terminal Rho GAP domain, which was cloned from mouse brain mRNA using reverse transcriptase polymerase chain reaction. Comparison of the mouse with the human p190-B proteins revealed that approx. 97% of the amino acid residues were identical. Northern analysis of total RNA from a variety of mouse tissues detected ubiquitous expression of two p190-B transcripts of 4.0 and 6.8 kb in size. Analysis of two multilocus genetic crosses localized the mouse gene, Gfi2, to a position on chromosome 12, consistent with the mapping of the human gene to a position of conserved synteny on chromosome 14. The high level of sequence homology between the human and the mouse suggests that there is a strong selective pressure to maintain the p190-B protein structure.
- Subjects :
- Amino Acid Sequence
Animals
Base Sequence
Chromosome Mapping
Cloning, Molecular
DNA, Complementary chemistry
DNA-Binding Proteins
Exons
GTP Phosphohydrolases chemistry
GTPase-Activating Proteins
Mice
Molecular Sequence Data
Nuclear Proteins chemistry
Phosphoproteins chemistry
Repressor Proteins
GTP Phosphohydrolases genetics
Guanine Nucleotide Exchange Factors
Nuclear Proteins genetics
Phosphoproteins genetics
Subjects
Details
- Language :
- English
- ISSN :
- 0006-3002
- Volume :
- 1443
- Issue :
- 1-2
- Database :
- MEDLINE
- Journal :
- Biochimica et biophysica acta
- Publication Type :
- Academic Journal
- Accession number :
- 9838117
- Full Text :
- https://doi.org/10.1016/s0167-4781(98)00207-3