Comparative Study
doi: 10.1093/oxfordjournals.molbev.a040372.
Sequence of the ebgA gene of Escherichia coli: comparison with the lacZ gene
Affiliations
- PMID: 3939707
- DOI: 10.1093/oxfordjournals.molbev.a040372
Item in Clipboard
Comparative Study
Sequence of the ebgA gene of Escherichia coli: comparison with the lacZ gene
Mol Biol Evol.
1985 Nov.
Abstract
We have sequenced the ebgA (evolved beta-galactosidase) gene of Escherichia coli K12. The sequence shows 50% nucleotide identity with the E. coli lacZ gene, demonstrating that the two genes are related by descent from a common ancestral gene. Comparison of the two sequences suggests that the ebgA gene has recently been under selection. A significant excess of identical, rather than synonymous, codons used to encode identical amino acids at the same positions in the aligned sequences implies that some form of selection is operating directly at the DNA level. This selection is independent of, and in addition to, selection based on codon usage or on function of the gene products.
Similar articles
-
Sequence of the ebgR gene of Escherichia coli: evidence that the EBG and LAC operons are descended from a common ancestor.Mol Biol Evol. 1985 Nov;2(6):478-83. doi: 10.1093/oxfordjournals.molbev.a040373. Mol Biol Evol. 1985. PMID: 3939708
-
Expression and nucleotide sequence of the Lactobacillus bulgaricus beta-galactosidase gene cloned in Escherichia coli.J Bacteriol. 1989 Feb;171(2):625-35. doi: 10.1128/jb.171.2.625-635.1989. J Bacteriol. 1989. PMID: 2492511 Free PMC article.
-
Analysis of the lacZ sequences from two Streptococcus thermophilus strains: comparison with the Escherichia coli and Lactobacillus bulgaricus beta-galactosidase sequences.J Gen Microbiol. 1991 Feb;137(2):369-80. doi: 10.1099/00221287-137-2-369. J Gen Microbiol. 1991. PMID: 1901904
-
Experimental evolution of Ebg enzyme provides clues about the evolution of catalysis and to evolutionary potential.FEMS Microbiol Lett. 1999 May 1;174(1):1-8. doi: 10.1111/j.1574-6968.1999.tb13542.x. FEMS Microbiol Lett. 1999. PMID: 10234816 Review.
-
Escherichia coli promoter sequences: analysis and prediction.Methods Enzymol. 1996;273:30-42. doi: 10.1016/s0076-6879(96)73004-5. Methods Enzymol. 1996. PMID: 8791597 Review. No abstract available.
Cited by
-
Antarctic Rahnella inusitata: A Producer of Cold-Stable β-Galactosidase Enzymes.Int J Mol Sci. 2021 Apr 16;22(8):4144. doi: 10.3390/ijms22084144. Int J Mol Sci. 2021. PMID: 33923711 Free PMC article.
-
Beta-galactosidases (Escherichia coli) with double substitutions show that Tyr-503 acts independently of Glu-461 but cooperatively with Glu-537.J Protein Chem. 2003 Nov;22(7-8):663-8. doi: 10.1023/b:jopc.0000008731.16884.22. J Protein Chem. 2003. PMID: 14714733
-
Molecular and biochemical analysis of two beta-galactosidases from Bifidobacterium infantis HL96.Appl Environ Microbiol. 2001 Sep;67(9):4256-63. doi: 10.1128/AEM.67.9.4256-4263.2001. Appl Environ Microbiol. 2001. PMID: 11526031 Free PMC article.
-
Linkage map of Escherichia coli K-12, edition 10: the traditional map.Microbiol Mol Biol Rev. 1998 Sep;62(3):814-984. doi: 10.1128/MMBR.62.3.814-984.1998. Microbiol Mol Biol Rev. 1998. PMID: 9729611 Free PMC article. Review.
-
Directed evolution of a fucosidase from a galactosidase by DNA shuffling and screening.Proc Natl Acad Sci U S A. 1997 Apr 29;94(9):4504-9. doi: 10.1073/pnas.94.9.4504. Proc Natl Acad Sci U S A. 1997. PMID: 9114019 Free PMC article.
Publication types
MeSH terms
Substances
Associated data
- Actions
Grants and funding
LinkOut - more resources
Full Text Sources
Molecular Biology Databases
