The N-terminal domain of MuB protein has striking structural similarity to DNA-binding domains and mediates MuB filament–filament interactions-Reference-Cited by-同舟云学术

The N-terminal domain of MuB protein has striking structural similarity to DNA-binding domains and mediates MuB filament–filament interactions

Published:2015-08 Issue:2 Volume:191 Page:100-111
ISSN:1047-8477
Container-title:Journal of Structural Biology
language:en
Short-container-title:Journal of Structural Biology

Author:

Dramićanin Marija,López-Méndez Blanca,Boskovic Jasminka,Campos-Olivas Ramón,Ramón-Maiques Santiago

Publisher

Elsevier BV

Subject

Structural Biology

Reference48 articles.

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3. Steady-state kinetic analysis of ATP hydrolysis by the B protein of bacteriophage mu. Involvement of protein oligomerization in the ATPase cycle;Adzuma;J. Biol. Chem.,1991

4. The solution structure of the Oct-1 POU-specific domain reveals a striking similarity to the bacteriophage lambda repressor DNA-binding domain;Assa-Munt;Cell,1993

5. MuB protein allosterically activates strand transfer by the transposase of phage Mu;Baker;Cell,1991

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1. Elucidating the Architectural dynamics of MuB filaments in bacteriophage Mu DNA transposition;Nature Communications;2024-07-31

2. Deep sequencing reveals new roles for MuB in transposition immunity and target-capture, and redefines the insular Ter region of E. coli;Mobile DNA;2020-07-09

3. Mu Transposition in the Absence of the Target-capture Protein MuB Reveals New Roles of MuB in Target Immunity and Target Selection, and Redraws the Boundaries of the Insular Ter Region of E. coli;2020-04-25

4. Target DNA bending by the Mu transpososome promotes careful transposition and prevents its reversal;eLife;2017-02-13