Sequence of a cDNA from Drosophila coding for the 16 kD proteolipid component of the vacuolar H(+)-ATPase.
Sequence of a cDNA from Drosophila coding for the 16 kD proteolipid component of the vacuolar H(+)-ATPase.
复制标题
来自果蝇的 cDNA 序列,编码液泡 H( )-ATP 酶的 16 kD 蛋白脂质成分。
作者:
L. Meagher;P. Mclean;M. Finbow
The vacuolar H +-ATPases are a class of endomembrane pumps which acidify the interiors of vacuolar compartments of eukaryotic cells'. The major membrane component is a proteolipid of MW l6kD and the deduced amino acid sequences from a yeast gene 2 and from a bovine cDNA3 show high identity with each other and a lower identity with the 8kD subunit c proteolipid of the FIFOH+-ATP synthase. A related, possibly identical l6kD protein has also been found to be a component of gap junction-like structures isolated from animal tissues4. We have isolated a cDNA from Drosophila coding for the 16kD proteolipid as part of a study to understand the structure and disposition of this protein in the bilayer. A bovine cDNA coding for the 16kD proteolipid was first obtained by screening a commercially available cDNA library from adrenal medulla using oligonucleotide probes derived from the published sequence3. The Drosophila cDNA was identified from a larval library in lambda gtlO by screening with randomly primed probes from the bovine cDNA. The deduced amino acid sequence of the longest open reading frame from the Drosophila cDNA shows a high degree of identity with the bovine and yeast sequences and with the direct amino acid sequence of the gap junction form of the Nephrops norvegicus l6kD proteolipid (Finbow et al., unpublished results). We to the kind gift of the Drosophila larval cDNA library. This work was by the Cancer Research Campaign.