HIGH PLASTICITY OF MULTISPECIFIC DNA METHYLTRANSFERASES IN THE REGION CARRYING DNA TARGET RECOGNIZING ENZYME MODULES

被引:28
作者
WALTER, J [1 ]
TRAUTNER, TA [1 ]
NOYERWEIDNER, M [1 ]
机构
[1] MAX PLANCK INST MOLEC GENET,IHNESTR 73,W-1000 BERLIN 33,GERMANY
关键词
DNA METHYLTRANSFERASE; DNA SEQUENCE RECOGNITION; PROTEIN DNA INTERACTION; PROTEIN STRUCTURE; SPECIFICITY MODULES;
D O I
10.1002/j.1460-2075.1992.tb05545.x
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Multispecific cytosine C5 DNA methyltransferases (MTases) methylate more than one specific DNA target. This is due to the presence of several target recognizing domains (TRDs) in these enzymes. Such TRDs form part of a variable centre in the MTase primary sequence, which separates conserved enzyme core sequences responsible for general steps in the methylation reaction. By deleting, rearranging and exchanging several TRDs of multispecific MTases, we demonstrate their modular character; they mediate target recognition independent of a particular TRD or core sequence context. We show also that multispecific MTases can accommodate inert material of non-MTase origin within their variable region without losing their activity. The remarkable plasticity with respect to the material that can be integrated into this region suggests that the enzyme core sequences preceding or following it form separable functional domains. In spite of the documented flexibility multispecific MTases could not be endowed with novel specificities by integration of putative TRDs of monospecific MTases, pointing to differences between multi- and monospecific MTases in the way their core and TRD sequences interact.
引用
收藏
页码:4445 / 4450
页数:6
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