Processing of a plant vacuolar protein precursor in vitro - PubMed (original) (raw)
Processing of a plant vacuolar protein precursor in vitro
T Hattori et al. Eur J Biochem. 1987.
Free article
Abstract
A precursor for sporamin A, the storage protein of the tuberous roots of sweet potato deposited in the vacuole, is synthesized on membrane-bound polysomes and has an extra peptide of 37 amino acids at the N-terminus of the mature form, which can be divided into an N-terminal putative signal peptide sequence (residues -37 to -17) and a segment enriched with charged amino acids (residues -16 to -1) [Hattori, T., et al. (1985) Plant Mol. Biol. 5, 313-320]. We examined the in vitro processing of the sporamin A precursor using a messenger RNA derived from a full-length cDNA by the SP6 transcription system. When the in vitro translation in a wheat germ cell-free system was carried out in the presence of dog pancreas microsomal membranes, the precursor polypeptide (Mr = 24,000) was processed into an intermediate form still larger than the mature polypeptide (Mr = 20,000). The processed intermediate form was also produced by addition of microsomal membranes from sweet potato and potato in the translation reaction, although less efficiently compared to dog membranes. Moreover, Escherichia coli cells expressing sporamin precursor accumulated a polypeptide with the same electrophoretic mobility as the intermediate form produced in vitro. The processing by dog membranes is accompanied by translocation of the polypeptide across the membranes as assayed by resistance to externally added proteases. The N-terminal amino acid sequencing analysis of [3H]leucine-labelled intermediate form produced in vitro by dog membranes indicated that co-translational processing of the sporamin precursor by endoplasmic reticulum membranes removes only the signal peptide segment from the extra peptide, and suggested that the charged segment following the signal peptide is removed post-translationally during the transport of sporamin into vacuole. The significance of two-step processing of plant vacuolar protein precursor is discussed in relation to the two-step processing of precursors for yeast vacuolar proteins and animal lysosomal proteins.
Similar articles
- Vacuolar targeting and posttranslational processing of the precursor to the sweet potato tuberous root storage protein in heterologous plant cells.
Matsuoka K, Matsumoto S, Hattori T, Machida Y, Nakamura K. Matsuoka K, et al. J Biol Chem. 1990 Nov 15;265(32):19750-7. J Biol Chem. 1990. PMID: 2246259 - O-glycosylation of a precursor to a sweet potato vacuolar protein, sporamin, expressed in tobacco cells.
Matsuoka K, Watanabe N, Nakamura K. Matsuoka K, et al. Plant J. 1995 Dec;8(6):877-89. doi: 10.1046/j.1365-313x.1995.8060877.x. Plant J. 1995. PMID: 8580960 - Mechanism of compartmentation of secretory proteins: transport of exocrine pancreatic proteins across the microsomal membrane.
Scheele G, Jacoby R, Carne T. Scheele G, et al. J Cell Biol. 1980 Dec;87(3 Pt 1):611-28. doi: 10.1083/jcb.87.3.611. J Cell Biol. 1980. PMID: 7462318 Free PMC article. - Ribonucleoparticle-independent transport of proteins into mammalian microsomes.
Zimmermann R, Zimmermann M, Wiech H, Schlenstedt G, Müller G, Morel F, Klappa P, Jung C, Cobet WW. Zimmermann R, et al. J Bioenerg Biomembr. 1990 Dec;22(6):711-23. doi: 10.1007/BF00786927. J Bioenerg Biomembr. 1990. PMID: 2092035 Review. - Intracellular precursor forms of plasma proteins: their functions and possible occurrence in plasma.
Peters T Jr. Peters T Jr. Clin Chem. 1987 Aug;33(8):1317-25. Clin Chem. 1987. PMID: 3301066 Review.
Cited by
- In vitro processing of tomato proteinase inhibitor I by barley microsomal membranes: a system for analysis of cotranslational processing of plant endomembrane proteins.
Osteryoung KW, Sticher L, Jones RL, Bennett AB. Osteryoung KW, et al. Plant Physiol. 1992 Jun;99(2):378-82. doi: 10.1104/pp.99.2.378. Plant Physiol. 1992. PMID: 16668894 Free PMC article. - In vitro synthesis and processing of tomato fruit polygalacturonase.
Dellapenna D, Bennett AB. Dellapenna D, et al. Plant Physiol. 1988 Apr;86(4):1057-63. doi: 10.1104/pp.86.4.1057. Plant Physiol. 1988. PMID: 16666031 Free PMC article. - Large alkyl side-chains of isoleucine and leucine in the NPIRL region constitute the core of the vacuolar sorting determinant of sporamin precursor.
Matsuoka K, Nakamura K. Matsuoka K, et al. Plant Mol Biol. 1999 Dec;41(6):825-35. doi: 10.1023/a:1006357413084. Plant Mol Biol. 1999. PMID: 10737147 - Identification and expression of Pen c 2, a novel allergen from Penicillium citrinum.
Chow LP, Su NY, Yu CJ, Chiang BL, Shen HD. Chow LP, et al. Biochem J. 1999 Jul 1;341 ( Pt 1)(Pt 1):51-9. Biochem J. 1999. PMID: 10377244 Free PMC article. - Deposition of storage proteins.
Müntz K. Müntz K. Plant Mol Biol. 1998 Sep;38(1-2):77-99. Plant Mol Biol. 1998. PMID: 9738961 Review.
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources