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• W194348575 endingPage "3059" @default.
• W194348575 startingPage "3051" @default.
• W194348575 abstract "The Mu in vitro strand transfer reaction proceeds via two stable higher order nucleoprotein complexes, the Type 1 and Type 2 transpososomes. The Mu A protein is responsible for the structural and functional integrity of the Type 1 transpososome. We have investigated the quaternary structure of the Mu A protein within this complex by chemical cross-linking experiments and found that the basic structural unit is an A tetramer. Three Mu A binding sites in the transpososome are protected by DNase I footprinting: the outermost A binding sites L1 and R1, as well as R2. Genetic evidence is also presented which corroborates this result. Efficient formation of Type 1 complexes occurs in mini-Mus with the L3 or R3 sites deleted or when the L2 site has been substituted; but no reaction occurs in the absence of R2. The protection at the L1 and R1 sites extends 12-13 bp beyond the Mu-host junctions as seen by DNase I and methidiumpropyl-EDTA.Fe(II) [MPE.Fe(II)] foot-printing, indicating Mu A contacts with the flanking host sequences in the transpososome but not on linear DNA; furthermore, hydroxyl radical footprinting shows an unprecedentedly large enhancement on the continuous strand, 2 bp beyond the nick site outside the Mu right end, which suggests that an altered DNA structure is induced upon Type 1 complex formation." @default.
• W194348575 created "2016-06-24" @default.
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• W194348575 date "1991-10-01" @default.
• W194348575 modified "2023-10-18" @default.
• W194348575 title "Structural aspects of a higher order nucleoprotein complex: induction of an altered DNA structure at the Mu-host junction of the Mu type 1 transpososome." @default.
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• W194348575 doi "https://doi.org/10.1002/j.1460-2075.1991.tb07856.x" @default.
• W194348575 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/453020" @default.
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• W194348575 hasPublicationYear "1991" @default.
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