Two separate genes encode the catalytic 70 kDa V-ATPase subunit in Psilotum and Equisetum.

نویسندگان

  • T Starke
  • T P Linkkila
  • J P Gogarten
چکیده

Vacuolar type ATPases have been found on various endomembranes of eukaryotic cells, e.g. lysosomes, chromaffin granules, vesicles derived from the Golgi apparatus, endosomes and vacuoles. Although this ATPase type is targeted to different compartments in one cell, only one gene for each subunit had been found per genome. Using PCR across intron-exon boundaries we show that two different genes encode the catalytic subunit of the V-ATPase in Psilotum nudum and Equisetum arvense. The substitution rates for the three codon positions and the intervening sequences show that in Psilotum both genes are transcribed and are under selection pressure, however, this seems not to be the case for Equisetum. The relatively high similarity between the two genes found in each species as compared to the interspecies similarities suggest that for some time after the gene duplication had occurred the two copies were subject to gene conversion mechanisms. An unexpected degree of conservation of the intervening sequences themselves is noted and statistically verified, however, no structural constraints that could explain these findings were detected.

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

منابع مشابه

Composition and assembly of the yeast vacuolar H(+)-ATPase complex.

The proton-translocating ATPase (H(+)-ATPase) found on the membrane of the yeast vacuole is the best characterized member of the V-type ATPase family. Biochemical and genetic screens have led to the identification of 14 genes, the majority designated VMA (for vacuolar membrane ATPase) encoding subunits of the enzyme complex. At least eight genes encode for proteins comprising the peripherally a...

متن کامل

Multigene phylogeny of land plants with special reference to bryophytes and the earliest land plants.

A widely held view of land plant relationships places liverworts as the first branch of the land plant tree, whereas some molecular analyses and a cladistic study of morphological characters indicate that hornworts are the earliest land plants. To help resolve this conflict, we used parsimony and likelihood methods to analyze a 6, 095-character data set composed of four genes (chloroplast rbcL ...

متن کامل

Cloning, sequencing and expression of a novel cDNA encoding human vacuolar ATPase (14-kDa subunit).

A cDNA encoding the 14-kDa subunit of vacuolar ATPase was cloned from human fetal brain. The sequence was composed of 680 nucleotides containing an open reading frame of 357 nucleotides. The deduced peptide sequence consisted of 119 amino acid residues with a calculated molecular weight of 13,369 Da and a pI of 5.19. Overall, this amino-acid sequence was respectively 69% and 70% identical to th...

متن کامل

VACUOLAR-TYPE H+-TRANSLOCATING ATPases IN PLANT ENDOMEMBRANES: SUBUNIT ORGANIZATION AND MULTIGENE FAMILIES.

Acidification of endomembrane compartments by the vacuolar-type H+-translocating ATPase (V-ATPase) is vital to the growth and development of plants. The V-ATPase purified from oat roots is a large complex of 650x10(3 )Mr that contains 10 different subunits of 70, 60, 44, 42, 36, 32, 29, 16, 13 and 12x10(3 )Mr. This set of ten polypeptides is sufficient to couple ATP hydrolysis to proton pumping...

متن کامل

Structure of an ATPase operon of an acidothermophilic archaebacterium, Sulfolobus acidocaldarius.

The nucleotide sequence of the operon of the ATPase complex of an acidothermophilic archaebacterium, Sulfolobus acidocaldarius, has been determined. In addition to the three previously reported genes for the alpha, beta, and c (proteolipid) subunits of the ATPase complex (Denda, K., Konishi, J., Oshima, T., Date, T., and Yoshida, M. (1989) J. Biol. Chem. 264, 7119-7121), the operon contained th...

متن کامل

ذخیره در منابع من


  با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

عنوان ژورنال:
  • Zeitschrift fur Naturforschung. C, Journal of biosciences

دوره 46 7-8  شماره 

صفحات  -

تاریخ انتشار 1991