Abstract
The protein population of cassava root layers was characterized bySDS-PAGE and bidimensional polyacrylamide gel electrophoresis. SDS-Pagerevealed the presence of a protein population in the molecular weight rangebetween 94 and 20 kDa. The expression pattern of these proteins was welldefined within the different layers. Partial protein sequence analyses andpreliminary results on the layer-specific expression pattern obtained withNorthern analyses are presented.
Similar content being viewed by others
References
Puonti-Kaerlas J (1998) Cassava biotechnology. Biotech, Genet Enging Rev 15: 329–364.
Cock JH (1985) Cassava: A basic energy source in the tropics. In Cock JH, Reyes JA (eds), Cassava: Research, Production and Utilization. UNDP CIAT.
Li HQ, Sautter C, Potrykus I, Puonti-Kaerlas J (1996) Genetic transformation of cassava (Manihot esculenta Crantz). Nature Biotech 14: 736–740.
Rosahl S, Schmidt R, Schell J, Willmitzer L (1986) Isolation and characterization of a gene from Solanum tuberosum encoding patatin, the major storage protein of potato tubers. Mol Gen Genet 203: 230–236.
de Castro LA, Carneiro M, de C Neshich D, de Paiva GR (1992) Spatial and temporal gene expression patterns occur during corm development. Plant Cell 4(12): 1549–1559.
Bezerra IC, de Castro LA, Neshich G, de Almeida ER, de Sá MF, Mello LV, Monte-Neshich DC (1995) A corm-specific gene encodes tarin, a major globulin of taro (Colocasia esculenta L. Schott). Plant Mol Biol 28(1): 137–144.
Salehuzzaman SNIM, Jacobsen E, Visser RGF (1992) Cloning, partial sequencing and expression of a cDNA coding for branching enzyme in cassava. Plant Molec Biol 20: 809–819.
Cabral GB, Carvalho LJCB (2000) Cassava Biotechnology. IVth International Scientific Meeting-CBN. In Carvalho LJCB, Thro AM, Vilarinhos AD (eds), The Formation of Storage Root in Cassava. Published by Embrapa-Recursos Genéticos e Biotecnologia. Brasília-DF, Brazil, pp 345–356.
Ottoboni LMM, Leite A, Targon MLPN, Silva MJ, Arruda P (1990) Heterogenity of coix, maize and teosinte prolamins detected by isoelectric focusing. Revista Brasileira de Genética 13: 313–322.
Laemmli UK (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227: 680–685.
O'Farrel PH (1975) High resolution two dimensional electrophoresis of proteins. J Biol Chem 250: 4007–4021.
Jones JDG, Dunsumuir P, Bedbrook J (1985) High level expression of introduced chimaeric genes in regenerated transformed plants. EMBO J 4: 2411–2418.
Osborne TB (1908) Our present knowledge of plant proteins. Science 28: 412–427.
Lauzon LM, Helm KW, Vierling E (1990) A cDNA clone from Pisum sativum encoding a low molecular weight heat shock protein. Nucleic Acids Res 18(14): 4274.
Raschke E, Baumann G, Schoffl F (1988) Nucleotide sequence analysis of soybean small heat shock protein genes belonging to two different multigene families. J Mol Biol 199(4), 549–557.
Tseng TS, Yeh KW, Yeh CH, Chang FC, Chen YM, Lin CY (1992) Two rice (Oryza sativa) full-length cDNA clones encoding low-molecular-weight heat-shock proteins. Plant Mol Biol 18(5): 963–965.
Almoguera C, Jordano J (1992) Developmental and environmental concurrent expression of sunflower dry-seed-stored low-molecular-weight heat-shock protein and Lea mRNAs. Plant Mol Biol 19(5): 781–792.
Coca MA, Almoguera C, Jordano J (1994) Expression of sunflower low-molecular-weight heat-shock protein during embryogenesis and persistence after germination: localization and possible function implications. Plant Mol Biol 25: 479–492.
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
De Souza, C., Carvalho, L., De Almeida, E. et al. Identification of cassava root protein genes. Plant Foods Hum Nutr 57, 353–363 (2002). https://doi.org/10.1023/A:1021853000245
Issue Date:
DOI: https://doi.org/10.1023/A:1021853000245