Abstract:
:Mu DNA transposition proceeds through a series of higher-order nucleoprotein complexes called transpososomes. The structural core of the transpososome is a tetramer of the transposase, Mu A, bound to the two transposon ends. High-resolution structural analysis of the intact transposase and the transpososome has not been successful to date. Here we report the structure of Mu A at 16-angstroms and the Type 1 transpososome at 34-angstroms resolution, by 3D reconstruction of images obtained by scanning transmission electron microscopy (STEM) at cryo-temperatures. Electron spectroscopic imaging (ESI) of the DNA-phosphorus was performed in conjunction with the structural investigation to derive the path of the DNA through the transpososome and to define the DNA-binding surface in the transposase. Our model of the transpososome fits well with the accumulated biochemical literature for this intricate transposition system, and lays a structural foundation for biochemical function, including catalysis in trans and the complex circuit of macromolecular interactions underlying Mu DNA transposition.
journal_name
Genes Devjournal_title
Genes & developmentauthors
Yuan JF,Beniac DR,Chaconas G,Ottensmeyer FPdoi
10.1101/gad.1291405subject
Has Abstractpub_date
2005-04-01 00:00:00pages
840-52issue
7eissn
0890-9369issn
1549-5477pii
gad.1291405journal_volume
19pub_type
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