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Binding of Nicotiana nuclear proteins to the subterminal regions of the Ac transposable element
Year:
1996
Source of publication :
Molecular and General Genetics
Authors :
Fridlender, Marcelo
;
.
Volume :
251
Co-Authors:
Levy, A.A., Plant Genetics Department, Weizmann Institute of Science, Rehovot, 76100, Israel
Fridlender, M., Plant Genetics Department, Weizmann Institute of Science, Rehovot, 76100, Israel
Hanania, U., Plant Genetics Department, Weizmann Institute of Science, Rehovot, 76100, Israel, Botany Department, Tel Aviv University, Israel
Rubin, E., Plant Genetics Department, Weizmann Institute of Science, Rehovot, 76100, Israel
Sitrit, Y., Plant Genetics Department, Weizmann Institute of Science, Rehovot, 76100, Israel, Mann Laboratory, Department of Vegetable Crops, University of California, Davis, CA 95616, United States
Facilitators :
From page:
436
To page:
441
(
Total pages:
6
)
Abstract:
Specific binding of Nicotiana nuclear protein(s) to subterminal regions of the Ac transposable element was detected using gel mobility shift assays. A sequence motif (GGTAAA) repeated in both terminal regions of Ac, was identified as the protein binding site. Mutation of two nucleotides in this motif was sufficient to abolish binding. Based on a series of competition assays, it is deduced that there is cooperative binding between two repeats, each similar to the GGTAAA motif. The binding protein is probably similar to a previously characterized maize protein which binds to a GGTAAA-containing motif located in the ends of Mutator. Moreover, we show that DNA from Ds1 competes for protein binding to Ac termini, and we show, by sequence analysis, that GGTAAA binding sites are present in the terminal region of Tgm1, Tpn1, En/Spm, Tam3 and Ds1-like elements. This suggests that the binding protein(s) might be involved in the transposition process.
Note:
Related Files :
Base Sequence
DNA
DNA binding protein
Nicotiana
Nuclear Proteins
Plants, Toxic
structure activity relation
Transposition
Zea mays
Show More
Related Content
More details
DOI :
10.1007/s004380050187
Article number:
Affiliations:
Database:
Scopus
Publication Type:
article
;
.
Language:
English
Editors' remarks:
ID:
27393
Last updated date:
02/03/2022 17:27
Creation date:
17/04/2018 00:30
Scientific Publication
Binding of Nicotiana nuclear proteins to the subterminal regions of the Ac transposable element
251
Levy, A.A., Plant Genetics Department, Weizmann Institute of Science, Rehovot, 76100, Israel
Fridlender, M., Plant Genetics Department, Weizmann Institute of Science, Rehovot, 76100, Israel
Hanania, U., Plant Genetics Department, Weizmann Institute of Science, Rehovot, 76100, Israel, Botany Department, Tel Aviv University, Israel
Rubin, E., Plant Genetics Department, Weizmann Institute of Science, Rehovot, 76100, Israel
Sitrit, Y., Plant Genetics Department, Weizmann Institute of Science, Rehovot, 76100, Israel, Mann Laboratory, Department of Vegetable Crops, University of California, Davis, CA 95616, United States
Binding of Nicotiana nuclear proteins to the subterminal regions of the Ac transposable element
Specific binding of Nicotiana nuclear protein(s) to subterminal regions of the Ac transposable element was detected using gel mobility shift assays. A sequence motif (GGTAAA) repeated in both terminal regions of Ac, was identified as the protein binding site. Mutation of two nucleotides in this motif was sufficient to abolish binding. Based on a series of competition assays, it is deduced that there is cooperative binding between two repeats, each similar to the GGTAAA motif. The binding protein is probably similar to a previously characterized maize protein which binds to a GGTAAA-containing motif located in the ends of Mutator. Moreover, we show that DNA from Ds1 competes for protein binding to Ac termini, and we show, by sequence analysis, that GGTAAA binding sites are present in the terminal region of Tgm1, Tpn1, En/Spm, Tam3 and Ds1-like elements. This suggests that the binding protein(s) might be involved in the transposition process.
Scientific Publication
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