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Ricin A chain fused to a chloroplast-targeting signal is unfolded on the chloroplast surface prior to import across the envelope membranes
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UNSPECIFIED (1996) Ricin A chain fused to a chloroplast-targeting signal is unfolded on the chloroplast surface prior to import across the envelope membranes. JOURNAL OF BIOLOGICAL CHEMISTRY, 271 (8). pp. 4082-4085. ISSN 0021-9258.
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Abstract
The initial stages of chloroplast protein import involve the binding of precursor proteins to surface-bound receptors prior to translocation across the envelope membranes in a partially folded conformation, We have analyzed the unfolding process by examining the conformation of a construct, comprising the presequence of a chloroplast protein linked to ricin A chain, before and after binding to the chloroplast surface, We show that the presequence is highly susceptible to proteolysis in solution, probably reflecting a lack of tertiary structure, whereas the A chain passenger protein is resistant to extremely high concentrations of protease, unless deliberately unfolded using denaturant, The A chain moiety is furthermore active, indicating that the presence of the presequence does not prevent formation of a tightly folded, native state, In contrast, receptor-bound p33KRA (fusion protein comprising the 33-kDa presequence plus 22 residues of mature protein, linked to the A chain of ricin) is quantitatively digested by protease concentrations that have little effect on the A chain in solution, We conclude that protein unfolding can take place on the chloroplast surface in the absence of translocation and without the aid of soluble factors.
Item Type: | Journal Article | ||||
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Subjects: | Q Science > QD Chemistry | ||||
Journal or Publication Title: | JOURNAL OF BIOLOGICAL CHEMISTRY | ||||
Publisher: | AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC | ||||
ISSN: | 0021-9258 | ||||
Official Date: | 23 February 1996 | ||||
Dates: |
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Volume: | 271 | ||||
Number: | 8 | ||||
Number of Pages: | 4 | ||||
Page Range: | pp. 4082-4085 | ||||
Publication Status: | Published |
Data sourced from Thomson Reuters' Web of Knowledge
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