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Mutants of Ustilago maydis defective in production of one of two polypeptides of KP6 toxin from the preprotoxin
Year:
1993
Source of publication :
MGG Molecular & General Genetics
Authors :
Ginzberg, Idit
;
.
Volume :
238
Co-Authors:
Tao, J., Department of Biological Sciences, SUNY at Buffalo, Buffalo, 14260, NY, United States
Ginzberg, I., Department of Molecular Microbiology and Biotechnology, George Wise Faculty of Life Sciences, Tel Aviv University, Ramat Aviv, 69978, Israel
Koltin, Y., Department of Molecular Microbiology and Biotechnology, George Wise Faculty of Life Sciences, Tel Aviv University, Ramat Aviv, 69978, Israel
Bruenn, J.A., Department of Biological Sciences, SUNY at Buffalo, Buffalo, 14260, NY, United States
Facilitators :
From page:
234
To page:
240
(
Total pages:
7
)
Abstract:
Double-stranded RNA viruses of Ustilago maydis encode secreted killer toxins to which other cells of the same species and closely related species are sensitive. KP6 toxin consists of two polypeptides, α and β, produced from a single precursor preprotoxin. In this work, we cloned complementary DNA for the toxin-encoding segment of two of the KP6 nonkiller mutants NK3 and NK13 that secrete the β and α polypeptides, respectively. Both sequence analysis of the cDNA clones and in vitro translation of the toxin-encoding double-stranded RNAs showed that both mutants can produce full-length preprotoxins. Cys51 in α is converted to Arg in NK3 and Thr25 and Lys42 in β are changed to Pro and Arg, respectively, in NK13. Although α and β are encoded in a single prepropolypeptide, only the β polypeptide is secreted by NK3 and only the α polypeptide is secreted by NK 13. This differential expression of peptides from one precursor is a unique phenomenon. Neither of the nonsecreted polypeptides accumulated in the cytosol. The possible effects of these mutations on pre-protoxin folding and their consequences for toxin secretion are discussed. © 1993 Springer-Verlag.
Note:
Related Files :
Base Sequence
Molecular Sequence Data
mutation
polypeptide
Ustilago maydis killer toxin
Show More
Related Content
More details
DOI :
10.1007/BF00279552
Article number:
Affiliations:
Database:
Scopus
Publication Type:
article
;
.
Language:
English
Editors' remarks:
ID:
28903
Last updated date:
02/03/2022 17:27
Creation date:
17/04/2018 00:42
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Scientific Publication
Mutants of Ustilago maydis defective in production of one of two polypeptides of KP6 toxin from the preprotoxin
238
Tao, J., Department of Biological Sciences, SUNY at Buffalo, Buffalo, 14260, NY, United States
Ginzberg, I., Department of Molecular Microbiology and Biotechnology, George Wise Faculty of Life Sciences, Tel Aviv University, Ramat Aviv, 69978, Israel
Koltin, Y., Department of Molecular Microbiology and Biotechnology, George Wise Faculty of Life Sciences, Tel Aviv University, Ramat Aviv, 69978, Israel
Bruenn, J.A., Department of Biological Sciences, SUNY at Buffalo, Buffalo, 14260, NY, United States
Mutants of Ustilago maydis defective in production of one of two polypeptides of KP6 toxin from the preprotoxin
Double-stranded RNA viruses of Ustilago maydis encode secreted killer toxins to which other cells of the same species and closely related species are sensitive. KP6 toxin consists of two polypeptides, α and β, produced from a single precursor preprotoxin. In this work, we cloned complementary DNA for the toxin-encoding segment of two of the KP6 nonkiller mutants NK3 and NK13 that secrete the β and α polypeptides, respectively. Both sequence analysis of the cDNA clones and in vitro translation of the toxin-encoding double-stranded RNAs showed that both mutants can produce full-length preprotoxins. Cys51 in α is converted to Arg in NK3 and Thr25 and Lys42 in β are changed to Pro and Arg, respectively, in NK13. Although α and β are encoded in a single prepropolypeptide, only the β polypeptide is secreted by NK3 and only the α polypeptide is secreted by NK 13. This differential expression of peptides from one precursor is a unique phenomenon. Neither of the nonsecreted polypeptides accumulated in the cytosol. The possible effects of these mutations on pre-protoxin folding and their consequences for toxin secretion are discussed. © 1993 Springer-Verlag.
Scientific Publication
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