ArticlePlant molecular biology1995
Primary structure of the plasma membrane H(+)-ATPase from the halotolerant alga Dunaliella bioculata.
Article in Plant molecular biology, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
6 citing papers in PubMed, 19 citations in OpenAlex.
- Cloning and Characterization of Two Putative P-Type ATPases from the Marine MicroalgaPlants (Basel, Switzerland) · 2021Article
- Sodium, potassium-atpases in algae and oomycetes.Journal of bioenergetics and biomembranes · 2005Article
- Functional role of positively charged amino acid residues in the transmembrane segments of the yeast PMA1 ATPase.Folia microbiologica · 1998Article
- Primary structure and effect of pH on the expression of the plasma membrane H(+)-ATPase from Dunaliella acidophila and Dunaliella salina.Plant physiology · 1996Article
- Influence of photoheterotrophy on the expression of chlorophyll a/b-binding proteins in the green alga Pyrobotrys stellata.Photosynthesis research · 1996Article
- Molecular cloning of a P-type Ca(2+)-ATPase from the halotolerant alga Dunaliella bioculata.Planta · 1996Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 2 countries.
Funding
Abstract
P-type ATPase-specific oligodeoxyribonucleotides were used to obtain a fragment of the H(+)-ATPase of the salt tolerant alga Dunaliella bioculata by polymerase chain reaction (PCR). This fragment served as a probe in screening a cDNA-library from this organism. The complete primary structure of the ATPase protein (DBPMA1) was deduced from sequencing a 4.7 kb cDNA clone. The protein shows highest homology to H(+)-ATPases from higher plants and fungi (43% identity, 67% similarity) but has a higher calculated molecular mass (123 kDa). The latter can be assigned mainly to an additional hydrophilic domain between transmembrane segments VI and VII and to an extended carboxyterminus. These unusual structural features of DBPMA1 are interpreted in terms of providing regulatory sites of the enzyme. Southern blot analysis suggests the presence of only a single copy of the gene in the haploid D. bioculata genome. To investigate the role of the H(+)-ATPase in the adaption of D. bioculata to different external NaCl concentrations, we employed northern blot analyses. The results indicate that the pma1 transcript level of cells growing in salinities between 0.1 and 3 M NaCl is not directly correlated with the external salt concentration.
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