Cloning and characterization of a highly conserved HMG-like protein (PF16) gene from Plasmodium falciparum.
A novel gene encoding a protein of 147 amino acids (Pf16) has been cloned from Plasmodium falciparum and expressed in E. coli. The protein contains 19 methionines, all of which are localized in the NH2-terminal 35 amino acid residues, and it is also rich in lysine. Pf16 is highly basic, contains a polyacidic domain consisting of aspartic acid and is related to the non-histone high mobility group proteins of higher eukaryotes. The gene is conserved among eight different species of Plasmodium so far examined, suggesting an important function for this gene product in the parasite's life cycle.
Guntaka
R V
RV
Department of Molecular Microbiology and Immunology, School of Medicine, University of Missouri-Columbia 65212.
Kandala
J C
JC
Reddy
V D
VD
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D003001:Cloning, Molecular; D004247:DNA; D016054:DNA, Protozoan / Q000235:genetics* / Q000302:isolation & purification; D004926:Escherichia coli / Q000235:genetics; D015698:Genomic Library; D006609:High Mobility Group Proteins / Q000235:genetics*; D008969:Molecular Sequence Data; D010957:Plasmids; D010963:Plasmodium falciparum / Q000235:genetics*; D016133:Polymerase Chain Reaction; D015800:Protozoan Proteins / Q000235:genetics*; D051381:Rats; D015183:Restriction Mapping; D012689:Sequence Homology, Nucleic Acid; D014337:Trout
D016054:DNA, Protozoan; D006609:High Mobility Group Proteins; D015800:Protozoan Proteins; D004247:DNA