A conserved intron in the V‐ATPase <i>A</i> subunit genes of plants and algae

Starke, Thomas; Gogarten, J. Peter

doi:10.1016/0014-5793(93)81174-x

Cited by 24 publications

(15 citation statements)

References 40 publications

(29 reference statements)

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“…crystallinum subunits were used as homologous probes for Southern blot analysis, we obtained evidence for one or two genes for each subunit. In all higher plants tested, with the exception of A. thaliana, two genes are present for subunit A (Starke and Gogarten, 1993) as determined by intronspanning PCR. Similarly for subunits B and c, evidence has been obtained for the existence of isoforms in higher plants (Lai et al, 1991;Berkelman et al, 1994).…”

Section: Expression Of Vacuolar H + -Atpase Genes After Saltmentioning

confidence: 99%

Early Salt Stress Effects on the Differential Expression of Vacuolar H+-ATPase Genes in Roots and Leaves of Mesembryanthemum crystallinum

et al. 1996

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Section: Expression Of Vacuolar H + -Atpase Genes After Saltmentioning

confidence: 99%

Early Salt Stress Effects on the Differential Expression of Vacuolar H+-ATPase Genes in Roots and Leaves of Mesembryanthemum crystallinum

et al. 1996

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“…Although the complexity of the subunit c gene families clearly varies among species, all species analyzed thus far show a remarkable sequence conservation in the coding region [10,12,13,19]. Interestingly, Southern blot analysis for subunit A revealed only a single strongly hybridizing band, although many plant species appear to have more than one subunit A gene [22].…”

mentioning

confidence: 99%

Salt stress induces an increased expression of V-type H+-ATPase in mature sugar beet leaves

Kirsch¹,

Zhigang²,

Viereck³

et al. 1996

Plant Mol Biol

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In the halotolerant sugar beet co-expression of V-ATPase and a vacuolar Na+/H(+)-antiporter provides a mechanism for vacuolar salt sequestration. To analyze salt-induced changes in the expression of the vacuolar H(+)-ATPase (V-ATPase) a partial cDNA of the proton-channel forming subunit c was cloned by RT-PCR. Southern blot analysis indicated a small gene family. In control plants transcript levels were high in roots and young growing leaves but low in fully expanded leaves. In mature leaves salt exposure (400 mM, 48 h) induced a strong increase in subunit c-mRNA. Transcripts for the catalytic subunit A followed a similar developmental and stress-modulated pattern, indicating a coordinate regulation of transcripts for both V-ATPase subunits. Concomittant with the mRNA increases the amount of V-ATPase protein increased as well.

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“…In most land plants, two genes for the A subunit exist, the result of an ancient gene duplication event (Starke and Gogarten 1993). Even in Arabidopsis, which has only one functional A-subunit gene, genome analysis has revealed remnants of a second copy of the A-subunit gene (Sze et al 2002).…”

Section: Discussionmentioning

confidence: 99%

Two isoforms of the A�subunit of the vacuolar H+-ATPase in Lycopersicon esculentum: highly similar proteins but divergent patterns of tissue localization

Bageshwar

Taneja-Bageshwar

Moharram

et al. 2004

Planta

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The plant vacuolar H(+)-translocating ATPase (V-ATPase, EC 3.6.1.34) generates a H+ electro-chemical gradient across the tonoplast membrane. We isolated two full-length cDNA clones (VHA-A1 and VHA-A2) from tomato (Lycopersicon esculentum Mill. cv. Large Cherry Red) coding for two isoforms of the V-ATPase catalytic subunit (V-ATPases A1 and A2). The cDNA clones encoding the two isoforms share 90% identity at the nucleotide level and 96% identity at the amino acid level. The 5'- and 3'-untranslated regions, however, are highly diverse. Both V-ATPase A1 and A2 isoforms encode polypeptides of 623 amino acids, with calculated molecular masses of 68,570 and 68,715, respectively. The expression of VHA-A1 and accumulation of V-ATPase A1 polypeptide were ubiquitous in all tissues examined. In response to salinity, the abundances of both transcript (VHA-A1) and protein (V-ATPase A1) of the A1 isoform in leaves were nearly doubled. In contrast to the A1 isoform, VHA-A2 transcript and V-ATPase A2 polypeptide were only detected in abundance in roots, and in minor quantities in mature fruit. In roots, accumulation of transcripts and polypeptides did not change in response to salinity for either isoform. Subcellular localization indicated that the highest levels of both V-ATPase A1 and A2 isoforms were in the tonoplast. However, significant quantities of both isoforms were detected in membranes associated with endoplasmic reticulum and/or Golgi. Immunoprecipitation of dissociated V1 domains using isoform-specific antibodies showed that V1 domains consist of either V-ATPase A1 or A2 catalytic subunit isoforms.

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A conserved intron in the V‐ATPase A subunit genes of plants and algae

Cited by 24 publications

References 40 publications

Early Salt Stress Effects on the Differential Expression of Vacuolar H+-ATPase Genes in Roots and Leaves of Mesembryanthemum crystallinum

Early Salt Stress Effects on the Differential Expression of Vacuolar H+-ATPase Genes in Roots and Leaves of Mesembryanthemum crystallinum

Salt stress induces an increased expression of V-type H+-ATPase in mature sugar beet leaves

Two isoforms of the A�subunit of the vacuolar H+-ATPase in Lycopersicon esculentum: highly similar proteins but divergent patterns of tissue localization

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