J. Biol. Chem.

An Arabidopsis thaliana ATP sulfurylase cDNA (ASA1), encoding a putative chloroplastic isoform, has been cloned by functional complementation of a Saccharomyces cerevisiae (met3) ATP sulfurylase mutant which also has a poor sulfate transport capacity. Homologous complementation of the yeast mutant with the ATP sulfurylase gene restores both ATP sulfurylase function and sulfate transport. Heterologous complementation restores only ATP sulfurylase function as demonstrated by low [35S]sulfate influx measurements and selenate resistance. A structural relationship between ATP sulfurylase and sulfate membrane transporters in yeast is proposed. The sequence of ASA1 is homologous to deduced plant and animal ATP sulfurylase sequences. Analyses indicate a potential tyrosine phosphorylation site which is unique to higher eukaryote sequences. ASA1 is specified by a single copy gene that is part of a multigene family in A. thaliana. At least two ASA1 copies are found in Brassica napus plants. ASA1 transcripts were found in all organs examined, with the highest transcript abundance and ATP sulfurylase activity in leaves or cotyledons. Absence of sulfate from culture media transiently increased B. napus transcript abundance, indicating that initially, the response to sulfate deprivation is transcriptionally regulated.

Source:http://purl.uniprot.org/citations/8647819