Abstract
To understand the subcellular roles and the regulation of vacuolar H+-ATPases, we have begun to identify the genes encoding the major subunits and to determine their patterns of expression in Arabidopsis thaliana. Two distinct cDNAs (AVA-P1 and AVA-P2) and one genomic sequence (AVA-P3) encoding the 16 kDa subunit have been isolated. The 16 kDa proteolipid is a major component of the membrane integral sector that forms the proton conductance pathway and is required for assembly of the V-ATPase complex. Interestingly, the open reading frame of one full-length cDNA (AVA-P1) and a genomic sequence (AVA-P3) encoded an identical polypeptide of 164 amino acids with a molecular mass of 16570. The deduced amino acid sequences of the two cDNAs were nearly identical (99%) and hydropathy plots suggested a molecule with four membrane-spanning domains characteristic of V-ATPase proteolipids. The three genes differed mainly in their codon usage and in their 3′-untranslated regions. The coding region of the genomic sequence, AVA-P3, was interrupted by two introns located at the codons for Cys-26 and Arg-121. The presence of additional 16 kDa proteolipid genes was suggested from several polymerase chain reaction (PCR)-amplified fragments that differed from one another in the size of the second intron. PCR 1 had an intron of ca. 800 bp and its identity as AVA-P4, a fourth member of the gene family, was confirmed from sequence analyses of an EST cDNA. The mRNAs of three genes (AVA-P1, AVA-P2 and AVA-P3) were detected in Arabidopsis leaf, root, flower and silique; yet expression of AVA-P1 and AVA-P2 was lower in roots. All three genes were expressed in light- or dark-grown seedlings; however mRNA levels of AVA-P2 were enhanced in etiolated plants. Arabidopsis thaliana, there-fore, has at least four distinct genes encoding nearly identical 16 kDa proteolipids, and the enhanced expression of AVA-P2 transcript in etiolated seedlings suggests that an increase in V-ATPase could accompany cell expansion.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 227-244 |
| Number of pages | 18 |
| Journal | Plant Molecular Biology |
| Volume | 29 |
| Issue number | 2 |
| DOIs | |
| State | Published - Oct 1995 |
| Externally published | Yes |
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Keywords
- 16 kDa subunit
- Arabidopsis thaliana
- H-pumping ATPase
- multigene family
- proteolipid
- vacuolar-type
ASJC Scopus subject areas
- Biochemistry
- Biochemistry, Genetics and Molecular Biology(all)
Cite this
Several distinct genes encode nearly identical 16 kDa proteolipids of the vacuolar H+-ATPase from Arabidopsis thaliana. / Perera, Imara Y.; Li, Xuhang; Sze, Heven.
In: Plant Molecular Biology, Vol. 29, No. 2, 10.1995, p. 227-244.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Several distinct genes encode nearly identical 16 kDa proteolipids of the vacuolar H+-ATPase from Arabidopsis thaliana
AU - Perera, Imara Y.
AU - Li, Xuhang
AU - Sze, Heven
PY - 1995/10
Y1 - 1995/10
N2 - To understand the subcellular roles and the regulation of vacuolar H+-ATPases, we have begun to identify the genes encoding the major subunits and to determine their patterns of expression in Arabidopsis thaliana. Two distinct cDNAs (AVA-P1 and AVA-P2) and one genomic sequence (AVA-P3) encoding the 16 kDa subunit have been isolated. The 16 kDa proteolipid is a major component of the membrane integral sector that forms the proton conductance pathway and is required for assembly of the V-ATPase complex. Interestingly, the open reading frame of one full-length cDNA (AVA-P1) and a genomic sequence (AVA-P3) encoded an identical polypeptide of 164 amino acids with a molecular mass of 16570. The deduced amino acid sequences of the two cDNAs were nearly identical (99%) and hydropathy plots suggested a molecule with four membrane-spanning domains characteristic of V-ATPase proteolipids. The three genes differed mainly in their codon usage and in their 3′-untranslated regions. The coding region of the genomic sequence, AVA-P3, was interrupted by two introns located at the codons for Cys-26 and Arg-121. The presence of additional 16 kDa proteolipid genes was suggested from several polymerase chain reaction (PCR)-amplified fragments that differed from one another in the size of the second intron. PCR 1 had an intron of ca. 800 bp and its identity as AVA-P4, a fourth member of the gene family, was confirmed from sequence analyses of an EST cDNA. The mRNAs of three genes (AVA-P1, AVA-P2 and AVA-P3) were detected in Arabidopsis leaf, root, flower and silique; yet expression of AVA-P1 and AVA-P2 was lower in roots. All three genes were expressed in light- or dark-grown seedlings; however mRNA levels of AVA-P2 were enhanced in etiolated plants. Arabidopsis thaliana, there-fore, has at least four distinct genes encoding nearly identical 16 kDa proteolipids, and the enhanced expression of AVA-P2 transcript in etiolated seedlings suggests that an increase in V-ATPase could accompany cell expansion.
AB - To understand the subcellular roles and the regulation of vacuolar H+-ATPases, we have begun to identify the genes encoding the major subunits and to determine their patterns of expression in Arabidopsis thaliana. Two distinct cDNAs (AVA-P1 and AVA-P2) and one genomic sequence (AVA-P3) encoding the 16 kDa subunit have been isolated. The 16 kDa proteolipid is a major component of the membrane integral sector that forms the proton conductance pathway and is required for assembly of the V-ATPase complex. Interestingly, the open reading frame of one full-length cDNA (AVA-P1) and a genomic sequence (AVA-P3) encoded an identical polypeptide of 164 amino acids with a molecular mass of 16570. The deduced amino acid sequences of the two cDNAs were nearly identical (99%) and hydropathy plots suggested a molecule with four membrane-spanning domains characteristic of V-ATPase proteolipids. The three genes differed mainly in their codon usage and in their 3′-untranslated regions. The coding region of the genomic sequence, AVA-P3, was interrupted by two introns located at the codons for Cys-26 and Arg-121. The presence of additional 16 kDa proteolipid genes was suggested from several polymerase chain reaction (PCR)-amplified fragments that differed from one another in the size of the second intron. PCR 1 had an intron of ca. 800 bp and its identity as AVA-P4, a fourth member of the gene family, was confirmed from sequence analyses of an EST cDNA. The mRNAs of three genes (AVA-P1, AVA-P2 and AVA-P3) were detected in Arabidopsis leaf, root, flower and silique; yet expression of AVA-P1 and AVA-P2 was lower in roots. All three genes were expressed in light- or dark-grown seedlings; however mRNA levels of AVA-P2 were enhanced in etiolated plants. Arabidopsis thaliana, there-fore, has at least four distinct genes encoding nearly identical 16 kDa proteolipids, and the enhanced expression of AVA-P2 transcript in etiolated seedlings suggests that an increase in V-ATPase could accompany cell expansion.
KW - 16 kDa subunit
KW - Arabidopsis thaliana
KW - H-pumping ATPase
KW - multigene family
KW - proteolipid
KW - vacuolar-type
UR - http://www.scopus.com/inward/record.url?scp=0029379622&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0029379622&partnerID=8YFLogxK
U2 - 10.1007/BF00043648
DO - 10.1007/BF00043648
M3 - Article
C2 - 7579175
AN - SCOPUS:0029379622
VL - 29
SP - 227
EP - 244
JO - Plant Molecular Biology
JF - Plant Molecular Biology
SN - 0167-4412
IS - 2
ER -