The C-terminal portion of an archaeal toxin, aRelE, plays a crucial role in protein synthesis inhibition.
Mutations of amino acids in the C-terminal region of an archaeal toxin, aRelE, from Pyrococcus horikoshii were characterized with respect to protein synthesis inhibitory activity and 70S ribosome-binding activity. The results suggest that basic residues at the C-terminal region in aRelE play a crucial role both in 70S ribosome binding and in protein synthesis inhibition activities.
Kikutake
Chie
C
Laboratory of Structural Biology, Graduate School of Systems Life Sciences, Kyushu University, Fukuoka, Japan.
Shinohara
Masaaki
M
Takagi
Hisanori
H
Nakashima
Takashi
T
Kimura
Makoto
M
D019943:Amino Acid Substitution; D019843:Archaeal Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism / Q000633:toxicity*; D008958:Models, Molecular; D014176:Protein Biosynthesis / Q000187:drug effects*; D011487:Protein Conformation; D043902:Pyrococcus horikoshii; D012270:Ribosomes / Q000378:metabolism; D014118:Toxins, Biological / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism / Q000633:toxicity*
D019843:Archaeal Proteins; D014118:Toxins, Biological