Processed products of the hevein precursor in the latex of the rubber tree ( Hevea brasiliensis)

• Published in: FEBS letters Vol. 363; no. 3; pp. 211 - 213
• Main Authors: Soedjanaatmadja, Ukun M.S., Subroto, Toto, Beintema, Jaap J.
• Format: Journal Article
• Language: English
• Published: England Elsevier B.V 24.04.1995
• Subjects: Amino Acid Sequence; Antimicrobial Cationic Peptides; Hevea brasiliensis; Hevein; Latex - chemistry; Lectins - metabolism; Molecular Sequence Data; Plant Lectins; Plant Proteins - metabolism; Protein Precursors - metabolism; Protein processing; Protein Processing, Post-Translational; Sequence Alignment; Sequence Homology, Amino Acid; Trees; Vacuolar targeting; Hevea brasiliensis; Hevein; Protein processing; Vacuolar targeting
• ISSN: 0014-5793; 1873-3468
• DOI: 10.1016/0014-5793(95)00309-W

The 20 kDa precursor of hevein and its C-terminal 14 kDa domain have been isolated. Sequence analysis of the C-terminal tryptic peptides of these proteins and comparison with the cDNA sequence indicate that they represent mature forms from which a C-terminal propeptide, possibly involved in vacuolar targeting, has been removed. The molar ratio of hevein to the C-terminal domain in the lutoid-body fraction of rubber latex is about 30:1. This indicates that not only the pre- and propeptides but also the 14 kDa domain are removed by proteolysis or other processes in the latex vessel after the processing of hevein has taken place.