The primary sequence of Ricinus communis agglutinin. Comparison with ricin

Roberts, L. M., Lamb, F. I., Pappin, D. J., Lord, J. M. (December 1985) The primary sequence of Ricinus communis agglutinin. Comparison with ricin. J Biol Chem, 260 (29). pp. 15682-6. ISSN 0021-9258 (Print)0021-9258 (Linking)

URL: http://www.ncbi.nlm.nih.gov/pubmed/2999130

Abstract

A mixture of synthetic oligonucleotides representing all possible sequences of a peptide present in the ricin B chain has been used to screen a cDNA library constructed using ripening castor bean seed poly(A+) RNA. The eight largest recombinant plasmids selected, by hybridization, a single mRNA species whose translational product was identified as preprolectin by immunoprecipitation. Restriction enzyme analysis of these clones demonstrated that two classes were present representing sequences complementary to two distinct but closely related preprolectin mRNA species. The nucleotide sequence of the cloned cDNA from one of these classes encodes preproricin and has been presented elsewhere (Lamb, F. I., Roberts, L. M., and Lord, J. M., (1985) Eur. J. Biochem. 148, 265-270). The nucleotide sequence of the second class is presented here and shown to represent prepro-Ricinus communis agglutinin. The entire coding sequence was deduced from two overlapping cDNA clones having inserts of 1668 and 1151 base pairs. The coding region defines a preproprotein with a 24-amino acid N-terminal signal sequence preceding the A chain (266 amino acids) which is joined to the B chain (262 amino acids) by a 12-amino acid linking peptide. The protein was confirmed as R. communis agglutinin since the deduced B chain N-terminal sequence corresponds exactly with that determined for purified R. communis agglutinin B chain over a region where several residue differences occur in the ricin B chain. The nucleotide and deduced amino acid sequences of the R. communis agglutinin precursor are compared with those of the ricin precursor.

Item Type: Paper
Uncontrolled Keywords: Amino Acid Sequence Base Sequence DNA/analysis DNA Restriction Enzymes/metabolism Lectins/ analysis/genetics Macromolecular Substances Plant Lectins Protein Biosynthesis Protein Precursors/analysis RNA, Messenger/analysis Ricin/ analysis/genetics
Subjects: bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein characterization
CSHL Authors:
Communities: CSHL labs > Pappin lab
Depositing User: Matt Covey
Date: 15 December 1985
Date Deposited: 10 Sep 2014 14:24
Last Modified: 10 Sep 2014 14:24
Related URLs:
URI: https://repository.cshl.edu/id/eprint/30772

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