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Tuning the relative affinities for activating and repressing operators of a temporally regulated restriction-modification system.

Abstract：

:Most type II restriction-modification (R-M) systems produce separate endonuclease (REase) and methyltransferase (MTase) proteins. After R-M genes enter a new cell, MTase activity must appear before REase or the host chromosome will be cleaved. Temporal control of these genes thus has life-or-death consequences. PvuII and some other R-M systems delay endonuclease expression by cotranscribing the REase gene with the upstream gene for an autogenous activator/repressor (C protein). C.PvuII was previously shown to have low levels early, but positive feedback later boosts transcription of the C and REase genes. The MTase is expressed without delay, and protects the host DNA. C.PvuII binds to two sites upstream of its gene: O(L), associated with activation, and O(R), associated with repression. Even when symmetry elements of each operator are made identical, C.PvuII binds preferentially to O(L). In this study, the intra-operator spacers are shown to modulate relative C.PvuII affinity. In light of a recently reported C.Esp1396I-DNA co-crystal structure, in vitro and in vivo effects of altering O(L) and O(R) spacers were determined. The results suggest that the GACTnnnAGTC consensus is the primary determinant of C.PvuII binding affinity, with intra-operator spacers playing a fine-tuning role that affects mobility of this R-M system.

journal_name

Nucleic Acids Res

journal_title

Nucleic acids research

authors

Mruk I,Blumenthal RM

doi

10.1093/nar/gkn1010

subject

Has Abstract

pub_date

2009-02-01 00:00:00

pages

983-98

issue

3

eissn

0305-1048

issn

1362-4962

pii

gkn1010

journal_volume

37

pub_type

杂志文章

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