PROTEIN HU BINDS SPECIFICALLY TO KINKED DNA

被引:171
|
作者
PONTIGGIA, A
NEGRI, A
BELTRAME, M
BIANCHI, ME
机构
[1] UNIV MILAN,DIPARTIMENTO GENET & BIOL MICRORGAN,VIA CELORIA 26,I-20133 MILAN,ITALY
[2] OSPED SAN RAFFAELE,IST SCI,I-20132 MILAN,ITALY
[3] UNIV MILAN,IST FISIOL V & BIOCHIM,I-20133 MILAN,ITALY
关键词
D O I
10.1111/j.1365-2958.1993.tb01126.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
We have purified the main four-way junction DNA-binding protein of Escherichia coli, and have found it to be the well-known HU protein. HU protein recognizes with high-affinity one of the angles present in the junction, a molecule with the shape of an X. Other DNA structures characterized by sharp bends or kinks, like bulged duplex DNAs containing unpaired bases, are also bound. HU protein appears to inhibit cruciform extrusion from supercoiled inverted repeat (palindromic) DNA, either by constraining supercoiling or by trapping a metastable interconversion intermediate. All these properties are analogous to the properties of the mammalian chromatin protein HMG1. We suggest that HU is a prokaryotic HMG1-like protein rather than a histone-like protein.
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页码:343 / 350
页数:8
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