Premium
Primary structure of the α‐subunit of vacuolar‐type Na + ‐ATPase in Enterococcus hirae Amplification of a 1000‐bp fragment by polymerase chain reaction
Author(s) -
Yoshihiko Kakinuma,
Kazuei Igarashi,
Kiyoshi Kawai,
Ichiro Yamato
Publication year - 1991
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(91)80835-q
Subject(s) - enterococcus hirae , microbiology and biotechnology , atpase , protein subunit , oligonucleotide , biology , peptide sequence , biochemistry , amino acid , nucleic acid sequence , genomic dna , protein primary structure , dna , gene , enzyme , enterococcus , antibiotics
A 1000‐bp fragment of Enterococcus hirae genomic DNA was amplified by the polymerase chain reaction method, using the oligonucleotide primers designed from amino acid sequences of both amino‐terminal and a tryptic fragment of the Na + ‐ATPase α‐subunit in this organism. DNA sequencing of this product revealed that the amino acid sequence of Na + ‐ATPase α‐subunit is highly homologous to the corresponding sequences of large (α) subunits of vacuolar (archaebacterial) type H + ‐ATPases, supporting our proposal [Kakinuma, Y. and Igarashi, K. (1990) FEBS Lett. 271, 97–101] that the Na + ‐ATPase of this organism belongs to the vacuolar‐type ATPase.