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An attempt to unify the structure of polymerases
- Source :
- Protein Engineering, Design and Selection, Protein Engineering, Design and Selection, 1990, 3 (6), pp.461-467. ⟨10.1093/protein/3.6.461⟩
- Publication Year :
- 1990
- Publisher :
- HAL CCSD, 1990.
-
Abstract
- International audience; With the great availability of sequences from RNA- and DNA-dependent RNA and DNA polymerases, it has become possible to delineate a few highly conserved regions for various polymerase types. In this work a DNA polymerase sequence from bacteriophage SPO2 was found to be homologous to the polymerase domain of the Klenow fragment of polymerase I from Escherichia coli, which is known to be closely related to those from Staphylococcus pneumoniae, Thermus aquaticus and bacteriophages T7 and T5. The alignment of the SPO2 polymerase with the other five sequences considerably narrowed the conserved motifs in these proteins. Three of the motifs matched reasonably all the conserved motifs of another DNA polymerase type, characterized by human polymerase alpha. It is also possible to find these three motifs in monomeric DNA-dependent RNA polymerases and two of them in DNA polymerase beta and DNA terminal transferases. These latter two motifs also matched two of the four motifs recently identified in 84 RNA-dependent polymerases. From the known tertiary architecture of the Klenow fragment of E. coli pol I, a spatial arrangement can be implied for these motifs. In addition, numerous biochemical experiments suggesting a role for the motifs in a common function (dNTP binding) also support these inferences. This speculative hypothesis, attempting to unify polymerase structure at least locally, if not globally, under the pol I fold, should provide a useful model to direct mutagenesis experiments to probe template and substrate specificity in polymerases.
- Subjects :
- MESH: Mutation
DNA polymerase
Protein Conformation
DNA polymerase II
Staphylococcus
[SDV]Life Sciences [q-bio]
Molecular Sequence Data
Bioengineering
MESH: Amino Acid Sequence
MESH: Thermus
Biochemistry
Sensitivity and Specificity
MESH: Sequence Homology, Nucleic Acid
catalytic domain
Substrate Specificity
DNA polymerases
MESH: Protein Conformation
Sequence Homology, Nucleic Acid
RNA polymerase I
Escherichia coli
Amino Acid Sequence
structure
Thermus
Molecular Biology
Polymerase
Klenow fragment
MESH: DNA Polymerase I
Genetics
DNA clamp
MESH: Molecular Sequence Data
biology
Bacteria
MESH: Escherichia coli
RNA polymerases
MESH: Staphylococcus
DNA-Directed RNA Polymerases
DNA Polymerase I
MESH: Sensitivity and Specificity
MESH: DNA-Directed RNA Polymerases
MESH: Bacteria
Mutation
biology.protein
sequences
MESH: Substrate Specificity
DNA polymerase I
DNA polymerase mu
Biotechnology
Subjects
Details
- Language :
- English
- ISSN :
- 17410126 and 17410134
- Database :
- OpenAIRE
- Journal :
- Protein Engineering, Design and Selection, Protein Engineering, Design and Selection, 1990, 3 (6), pp.461-467. ⟨10.1093/protein/3.6.461⟩
- Accession number :
- edsair.doi.dedup.....68c6c566bd19384d7cd730c21b28b313
- Full Text :
- https://doi.org/10.1093/protein/3.6.461⟩