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J Biol Chem, Vol. 274, Issue 24, 17132-17138, June 11, 1999

Isolation, Characterization, and Functional Analysis of a Novel cDNA Clone Encoding a Small Rubber Particle Protein from Hevea brasiliensis

Soo Kyung Oh, Hunseung Kang, Dong Ho Shin, Jaemo Yang, Keng-See ChowDagger , Hoong Yeet YeangDagger , Birgit Wagner§, Heimo Breiteneder§, and Kyung-Hwan Han

From the Kumho Life and Environmental Science Laboratory, 1 Oryong-Dong, Puk-Gu, Kwangju 500-480, Korea, Dagger  Biotechnology and Strategic Research Unit, Rubber Research Institute of Malaysia, P.O. Box 10150, 50908 Kuala Lumpur, Malaysia, and § Department of General and Experimental Pathology, University of Vienna, AKH-EBO-3Q, Waehringer Guertel 18-20, Vienna 1090, Austria

Biochemical evidence reported so far suggests that rubber synthesis takes place on the surface of rubber particles suspended in the latex of Hevea brasiliensis. We have isolated and characterized a cDNA clone that encodes a protein tightly bound on a small rubber particle. We named this protein small rubber particle protein (SRPP). Prior to this study, this protein was known as a latex allergen, and only its partial amino acid sequence was reported. Sequence analysis revealed that this protein is highly homologous to the rubber elongation factor and the Phaseolus vulgaris stress-related protein. Southern and Northern analyses indicate that the protein is encoded by a single gene and highly expressed in latex. An allergenicity test using the recombinant protein confirmed that the cloned cDNA encodes the known 24-kDa latex allergen. Neither ethylene stimulation nor wounding changed the transcript level of the SRPP gene in H. brasiliensis. An in vitro rubber assay showed that the protein plays a positive role in rubber biosynthesis. Therefore, it is likely that SRPP is a part of the rubber biosynthesis machinery, if not the rubber polymerase, along with the rubber elongation factor.

Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.


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