@article{fdi:010012484, title = {{M}olecular characterization of the alpha-amylase genes of {L}actobacillus plantarum {A}6 and {L}actobacillus amylovorus reveals an unusual 3' end structure with direct tandem repeats and suggests a common evolutionary origin}, author = {{G}iraud, {E}ric and {C}uny, {G}{\'e}rard}, editor = {}, language = {{ENG}}, abstract = {{T}he alpha-amylase gene (amy{A}) of #{L}actobacillus plantarum$ {A}6 was isolated from the genome by polymerase chain reaction with degenerated oligonucleotides, synthesized according to the tryptic peptide amino acid sequences of the purified enzyme. {N}ucleic acid sequence analysis revealed one open reading frame of 2739 bp encoding a 913 amino acid protein. {T}he amylase appears to be divided into two equal parts. {T}he {N}-terminal part has the typical characteristics of the well-known alpha-amylase family (65% identity with the alpha-amylase of #{B}acillus subtilis$ and 97% identity with the partial sequence available for the alpha-amylase of #{L}actobacillus amylovorus$). {T}he {C}-terminal part displays a fairly unusual structure. {I}t consists of four direct tandem repeated sequences of 104 amino acids sharing 100% similarity. {T}he complete nucleotide sequence of the alpha-amylase gene of #{L}. amylovorus$ was also determined. {A}n open reading frame of 2862 bp encoding a 954 amino acid protein was identified. {P}erfect homology between the two amy{A} genes was observed in the {N}-terminal region. {T}he {C}-terminal part of #{L}. amylovorus$ alpha-amylase also included tandem repeat units but striking differences were observed : the addition of one repeat unit ; a shorter, 91 amino acid repetition unit. {T}hese structural homologies suggest that both genes have a common ancestor and may have evolved independently by duplication with subsequent recombination and mutation. ({R}{\'e}sum{\'e} d'auteur)}, keywords = {{MICROBIOLOGIE} ; {BACTERIE} {LACTIQUE} ; {ENZYME} ; {GENETIQUE} ; {TECHNIQUE} {PCR} ; {PHYLOGENIE}}, booktitle = {}, journal = {{G}ene}, numero = {198}, pages = {149--157}, ISSN = {0378-1119}, year = {1997}, DOI = {10.1016/{S}0378-1119(97)00309-0}, URL = {https://www.documentation.ird.fr/hor/fdi:010012484}, }