Structure and expression of a tandem gene pair in Leishmania donovani that encodes a protein structurally homologous to eucaryotic cation-transporting ATPases.
An oligonucleotide probe was used to clone a cation-transporting ATPase gene from the genome of Leishmania donovani. The nucleotide sequence of the gene contained a 2,922-base-pair open reading frame that was predicted to encode a 107,406-dalton protein composed of 974 amino acids. The predicted L. donovani protein contained all the structural and functional domains expected to be present in a cation-transporting ATPase of the aspartyl phosphate class. The nucleotide sequence encoding the ATPase gene was duplicated in tandem in the parasite genome. Partial sequenation of the second member of the tandem repeat, which lay 2 kilobase pairs downstream of the ATPase gene, indicated that it was either identical to the first gene or very closely related to it. RNA homologous to either the ATPase gene or its adjacent relative was 5 kilobases in size and was approximately equally abundant in both promastigote and amastigote forms of the organism.
Meade
J C
JC
Department of Microbiology and Molecular Genetics, University of Cincinnati Medical Center, Ohio 45267-0524.
Shaw
J
J
Lemaster
S
S
Gallagher
G
G
Stringer
J R
JR
D000251:Adenosine Triphosphatases / Q000235:genetics*; D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D003001:Cloning, Molecular; D004262:DNA Restriction Enzymes; D005796:Genes; D007893:Leishmania donovani / Q000201:enzymology / Q000235:genetics*; D008969:Molecular Sequence Data; D009710:Nucleotide Mapping; D012689:Sequence Homology, Nucleic Acid; D014158:Transcription, Genetic
D004262:DNA Restriction Enzymes; D000251:Adenosine Triphosphatases