Purification and characterization of Luffin P1, a ribosome-inactivating peptide from the seeds of Luffa cylindrica.
A peptide designated Luffin P1 was purified from the seeds of Luffa cylindrica. Its molecular mass was determined to be 5226.1 Da by MALDI-TOF MS analysis. The purified Luffin P1 shows a strong inhibitory activity on protein synthesis in the cell-free rabbit reticulocyte lysate with IC(50) of 0.88 nM. Its reaction mechanism is the same as that of the ribosome-inactivating protein trichosanthin, which is an rRNA N-glycosidase. Besides, the results of gel filtration chromatography suggested the existence of polymers of Luffin P1 and polymerization of Luffin P1 enhanced its rRNA N-glycosidase activity. Luffin P1 was the smallest peptide yet reported that has translational inhibitory activity. The cDNA and deduced amino acid sequence of Luffin P1 has also been determined.
Li
Feng
F
Key laboratory of Proteomics, Institute of Biochemistry and Cell Biology, Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences, 320 Yue-yang Road, Shanghai 200031, PR China.
Yang
Xin-xiu
XX
Xia
Hen-chuan
HC
Zeng
Rong
R
Hu
Wei-guo
WG
Li
Zhen
Z
Zhang
Zu-chuan
ZC
D000595:Amino Acid Sequence; D002474:Cell-Free System; D018076:DNA, Complementary / Q000235:genetics; D004591:Electrophoresis, Polyacrylamide Gel; D029776:Luffa / Q000737:chemistry*; D008970:Molecular Weight; D009699:N-Glycosyl Hydrolases / Q000378:metabolism; D010940:Plant Proteins / Q000737:chemistry / Q000235:genetics / Q000302:isolation & purification* / Q000494:pharmacology*; D014176:Protein Biosynthesis / Q000187:drug effects*; D054788:Ribosome Inactivating Proteins; D012270:Ribosomes / Q000187:drug effects* / Q000378:metabolism; D012639:Seeds / Q000737:chemistry*
D018076:DNA, Complementary; D010940:Plant Proteins; D009699:N-Glycosyl Hydrolases; D054788:Ribosome Inactivating Proteins