Nucleotide sequence and molecular evolution of the gene coding for glyceraldehyde-3-phosphate dehydrogenase in the thermoacidophilic Archaebacterium Sulfolobus solfataricus

A Sulfolobus solfataricus genomic library cloned in the EMBL3 phage was screened using as probes synthetic oligonucleotides designed from the known amino acid sequence of a peptide obtained from the purified glyceraldehyde-3-phosphate dehydrogenase (aGAPD) protein. The screening led to the isolation...

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Bibliographic Details
Published in:Biochemical genetics 1993-06, Vol.31 (5-6), p.241-251
Main Authors: ARCARI, P, DELLO RUSSO, A, IANNICIELLO, G, GALLO, M, BOCCHINI, V
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Base Sequence
Biological and medical sciences
Biological Evolution
DNA, Bacterial
Fundamental and applied biological sciences. Psychology
Genes, Bacterial
Genetic Code
Genetic Variation
Genetics of eukaryotes. Biological and molecular evolution
Glyceraldehyde-3-Phosphate Dehydrogenases - genetics
Molecular Sequence Data
Sequence Homology, Amino Acid
Space life sciences
Sulfolobus - enzymology
Sulfolobus - genetics
Sulfolobus solfataricus
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Summary:A Sulfolobus solfataricus genomic library cloned in the EMBL3 phage was screened using as probes synthetic oligonucleotides designed from the known amino acid sequence of a peptide obtained from the purified glyceraldehyde-3-phosphate dehydrogenase (aGAPD) protein. The screening led to the isolation of six recombinant phages (lambda G1-lambda G6) and one of them (lambda G4) contained the entire GAPD gene. The deduced amino acid sequence accounts for a protein made of 341 amino acids and the initial methionine is encoded by a GTG triplet. Alignment of the S. solfataricus aGAPD sequence versus GAPD from archaea, eukarya, and bacteria showed that aGAPD is very similar to other archaebacterial but not to eukaryotic or eubacterial GAPD. For known archaebacterial GAPD sequences, the rate of nucleotide substitutions per site per year showed that these sequences are homologous not only at the amino acid but also at the nucleotide level. The evolutionary rates are nearly similar to those reported for other eukaryotic genes.
ISSN:0006-2928
1573-4927
DOI:10.1007/BF00557333