Solution conformations of early intermediates in Mos1 transposition
| Autor: | V. Trevor Forsyth, Julia M. Richardson, Philip Callow, M.G. Cuypers, Maryia Trubitsyna |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2013 |
| Předmět: |
Transposable element
Models Molecular Stereochemistry Inverted Repeat Sequences Transposases Biology Cleavage (embryo) 03 medical and health sciences chemistry.chemical_compound X-Ray Diffraction Structural Biology Scattering Small Angle Tn10 Genetics Insertion sequence Transposase 030304 developmental biology 0303 health sciences 030302 biochemistry & molecular biology DNA Protein Structure Tertiary DNA-Binding Proteins Neutron Diffraction chemistry Composite transposon DNA Transposable Elements Dimerization |
| Zdroj: | 'Nucleic Acids Research ', vol: 41, pages: 2020-2033 (2013) Nucleic Acids Research Cuypers, M, Trubitsyna, M, Callow, P, Forsyth, V T & Richardson, J 2012, ' Solution conformations of early intermediates in Mos1 transposition ', Nucleic Acids Research, vol. 41, no. 3, pp. 2020-2033 . https://doi.org/10.1093/nar/gks1295 |
| ISSN: | 0305-1048 |
| Popis: | DNA transposases facilitate genome rearrangements by moving DNA transposons around and between genomes by a cut-and-paste mechanism. DNA transposition proceeds in an ordered series of nucleoprotein complexes that coordinate pairing and cleavage of the transposon ends and integration of the cleaved ends at a new genomic site. Transposition is initiated by transposase recognition of the inverted repeat sequences marking each transposon end. Using a combination of solution scattering and biochemical techniques, we have determined the solution conformations and stoichiometries of DNA-free Mos1 transposase and of the transposase bound to a single transposon end. We show that Mos1 transposase is an elongated homodimer in the absence of DNA and that the N-terminal 55 residues, containing the first helix-turn-helix motif, are required for dimerization. This arrangement is remarkably different from the compact, crossed architecture of the dimer in the Mos1 paired-end complex (PEC). The transposase remains elongated when bound to a single-transposon end in a pre-cleavage complex, and the DNA is bound predominantly to one transposase monomer. We propose that a conformational change in the single-end complex, involving rotation of one half of the transposase along with binding of a second transposon end, could facilitate PEC assembly. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|