Transposable Phage Mu

نویسندگان

چکیده

برای دانلود باید عضویت طلایی داشته باشید

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

منابع مشابه

Carboxyl Terminal Truncations of the Phage Mu Transposase

The Phage Mu transposase (MuA) is a 663 amino acid momomeric multidomain protein. A tetramer of MuA catalyzes the replicative transposition of Phage Mu. MuA pairs the ends of the Mu genome, cleaves the donor DNA and subsequently joins the Mu DNA to the target DNA in a concerted cleavage and joining reaction known as strand transfer. A series of truncations deleting 101, 136 and 173 amino acids ...

متن کامل

Solution structure of the I gamma subdomain of the Mu end DNA-binding domain of phage Mu transposase.

The MuA transposase of phase Mu is a large modular protein that plays a central role in transposition. We show that the Mu end DNA-binding domain, I beta gamma, which is responsible for binding the DNA attachment sites at each end of the Mu genome, comprises two subdomains, I beta and I gamma, that are structurally autonomous and do not interact with each other in the absence of DNA. The soluti...

متن کامل

Molecular model for the transposition and replication of bacteriophage Mu and other transposable elements.

A series of molecular events will explain how genetic elements can transpose from one DNA site to another, generate a short oligonucleotide duplication at both ends of the new insertion site, and replicate in the transposition process. These events include the formation of recombinant molecules which have been postulated to be intermediates in the transposition process. The model explains how t...

متن کامل

Characterization of the lysogenic repressor (c) from transposable Mu-like bacteriophage D108.

The c gene products from related, transposable phages Mu and D108 encode lysogenic repressors which negatively regulate transcription and transposition. Using the gel shift assay to monitor c-operator specific DNA-binding activity, the 19.5 kDa D108 c repressor was purified to homogeneity. Sequence analysis of the N-terminus confirmed the identity of the purified protein as the repressor and as...

متن کامل

ذخیره در منابع من


  با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید

ژورنال

عنوان ژورنال: Microbiology Spectrum

سال: 2014

ISSN: 2165-0497

DOI: 10.1128/microbiolspec.mdna3-0007-2014