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Molecular Biology

, Volume 52, Issue 5, pp 637–647 | Cite as

HMGB Proteins as DNA Chaperones That Modulate Chromatin Activity

  • A. L. Kozlova
  • M. E. Valieva
  • N. V. Maluchenko
  • V. M. Studitsky
REVIEWS

Abstract

HMGB proteins are involved in structural rearrangements caused by regulatory chromatin remodeling factors. Particular interest is attracted to a DNA chaperone mechanism, suggesting that the HMGB proteins introduce bends into the double helix, thus rendering DNA accessible to effector proteins and facilitating their activity. The review discusses the role that the HMBG proteins play in key intranuclear processes, including assembly of the preinitiation complex during transcription of ribosomal genes; transcription by RNA polymerases I, II, and III; recruitment of the SWI/SNF complex during transcription of nonribosomal genes; DNA repair; etc. The functions of the HMGB proteins are considered in detail with the examples of yeast HMO1 and NHP6. The two proteins possess unique features in adition to properties characteristic of the HMGB proteins. Thus, NHP6 stimulates a large-scale ATP-independent unwrapping of nucleosomal DNA by the FACT complex, while in its absence FACT stabilizes the nucleosome. HMO1 acts as an alternative linker histone. Both HMO1 and NHP6 are of applied interest primarly because they are homologs of human HMGB1, an important therapeutic target of anticancer and anti-inflammatory treatments.

Keywords:

chromatin nucleosome transcription transcription factors HMGB proteins HMO1 NHP6 HMGB1 SPT16 POB3 FACT 

Notes

ACKNOWLEDGMENTS

This work was supported by the Russian Science Foundation (project no. 14-24-00031).

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Copyright information

© Pleiades Publishing, Inc. 2018

Authors and Affiliations

  1. 1.Biological Faculty, Moscow State UniversityMoscowRussia
  2. 2.Cancer Epigenetics Program, Fox Chase Cancer CenterPhiladelphiaUSA

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