Abstract
ADP-ribosylation factors (ARFs) are ∼20-kDa guanine nucleotide-binding proteins that are allosteric activators of the NAD:arginine ADP-ribosyltransferase activity of cholera toxin and appear to play a role in intracellular vesicular trafficking. Although the physiological roles of these proteins have not been defined, it has been presumed that each has a specific intracellular function. To obtain genetic evidence that each ARF is under evolutionary pressure to maintain its structure, and presumably function, rat ARF cDNA clones were isolated and their nucleotide and deduced amino acid sequences were compared to those of other mammalian ARFs. Deduced amino acid sequences for rat ARFs 1, 2, 3, 5 and 6 were identical to those of the known cognate human and bovine ARFs; rat ARF4 was 96% identical to human ARF4. Nucleotide sequences of both the untranslated as well as the coding regions were highly conserved. These results indicate that the ARF proteins are, as a family, extraordinarily well conserved across mammalian species. The unusually high degree of conservation of the untranslated regions is consistent with these regions having important regulatory roles and that individual ARFs contain structurally unique elements required for specific functions.
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Abbreviations
- ARF:
-
ADP-ribosylation factor
- Gs :
-
the stimulatory heterotrimeric guanine nucleotide-binding protein associated with adenylyl cyclase
- SDS:
-
sodium dodecyl sulfate
- ORF:
-
open reading frame
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The nucleotide sequences reported in this manuscript were assigned the following accession numbers by GenBank. Rat ARF1, L12380; Rat ARF2, L12381; Rat ARF3, L12382; Rat ARF4, L12383; Rat ARF5, L12384; Rat ARF6, L12385.
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Russ Price, S., Nightingale, M.S., Tsuchiya, M. et al. Interspecies relationships among ADP-ribosylation factors (ARFs): Evidence of evolutionary pressure to maintain individual identities. Mol Cell Biochem 159, 15–23 (1996). https://doi.org/10.1007/BF00226058
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DOI: https://doi.org/10.1007/BF00226058