Evolution of the vacuolar H sup + -ATPase: Implications for the origin of eukaryotes

Journal Article · Fri Sep 01 04:00:00 EDT 1989 · Proceedings of the National Academy of Sciences of the United States of America; (USA)

DOI:https://doi.org/10.1073/pnas.86.17.6661· OSTI ID:7067072

Gogarten, J P; Kibak, H; Dittrich, P; Taiz, L; Bowman, E J; Bowman, B J ^[1]; Manolson, M F; Poole, R J ^[2]; Date, Takayasu ^[3]; Oshima, Tairo; Konishi, Jin; Denda, Kimitoshi; Yoshida, Masasuke ^[4]

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1. Univ. of California, Santa Cruz (USA)
2. McGill Univ., Montreal, Quebec (Canada)
3. Kanazawa Medical School, Ishikawa (Japan)
4. Tokyo Institute of Technology, Yokohama (Japan)

Active transport across the vaculoar components of the eukaryotic endomembrane system is energized by a specific vacuolar H{sup +}-ATPase. The amino acid sequences of the 70- and 60-kDa subunits of the vacuolar H{sup +}-ATPase are {approx}25% identical to the {beta} and {alpha} subunits, respectively, of the eubacterial-type F{sub 0}F{sub 1}-ATPases. The authors now report that the same vacuolar H{sup +}-ATPase subunits are {approx}50% identical to the {alpha} and {beta} subunits, respectively, of the sulfur-metabolizing Sulfolobus acidocaldarius, an archaebacterium (Archaeobacterium). Moreover, the homologue of an 88-amino acid stretch near the amino-terminal end of the 70-kDa subunit is absent from the F{sub 0}F{sub 1}-ATPase {beta} subunit but is present in the {alpha} subunit of Sulfolobus. Since the two types of subunits are homologous to each other, they must have arisen by a gene duplication that occurred prior to the last common ancestor of the eubacteria, eukaryotes, and Sulfolobus. Thus, the phylogenetic tree of the subunits can be rooted at the site where the gene duplication occurred. The inferred evolutionary tree contains two main branches: a eubacterial branch and an eocyte branch that gave rise to Sulfolobus and the eukaryotic host cell. The implication is that the vacuolar H{sup +}-ATPase of eukaryotes arose by the internalization of the plasma membrane H{sup +}-ATPase of an archaebacterial-like ancestral cell.

• DOE Contract Number: FG03-84ER13245
• OSTI ID: 7067072
• Journal Information: Proceedings of the National Academy of Sciences of the United States of America; (USA), Journal Name: Proceedings of the National Academy of Sciences of the United States of America; (USA) Vol. 86:17; ISSN 0027-8424; ISSN PNASA
• Country of Publication: United States
• Language: English

Related Subjects

550400* -- Genetics
59 BASIC BIOLOGICAL SCIENCES
ACID ANHYDRASES
AMINO ACID SEQUENCE
ATP-ASE
BACTERIA
BARYONS
BIOLOGICAL EVOLUTION
CELL CONSTITUENTS
CELL MEMBRANES
DNA SEQUENCING
ELEMENTARY PARTICLES
ENZYMES
FERMIONS
HADRONS
HYDROLASES
MEMBRANE TRANSPORT
MEMBRANES
MICROORGANISMS
MOLECULAR STRUCTURE
NUCLEONS
PHOSPHOHYDROLASES
PROTONS
STRUCTURAL CHEMICAL ANALYSIS