NDLI: Functional equivalence of HMGA- and histone H1-like domains in a bacterial transcriptional factor

Content Provider	PubMed Central
Author	Francisco, García-heras Padmanabhan, S. Murillo, Francisco J. Montserrat, Elías-arnanz
Abstract	Histone H1 and high-mobility group A (HMGA) proteins compete dynamically to modulate chromatin structure and regulate DNA transactions in eukaryotes. In prokaryotes, HMGA-like domains are known only in Myxococcus xanthus CarD and its Stigmatella aurantiaca ortholog. These have an N-terminal module absent in HMGA that interacts with CarG (a zinc-associated factor that does not bind DNA) to form a stable complex essential in regulating multicellular development, light-induced carotenogenesis, and other cellular processes. An analogous pair, CarDAd and CarGAd, exists in another myxobacterium, Anaeromyxobacter dehalogenans. Intriguingly, the CarDAd C terminus lacks the hallmark HMGA DNA-binding AT-hooks and instead resembles the C-terminal region (CTR) of histone H1. We find that CarDAd alone could not replace CarD in M. xanthus. By contrast, when introduced with CarGAd, CarDAd functionally replaced CarD in regulating not just 1 but 3 distinct processes in M. xanthus, despite the lower DNA-binding affinity of CarDAd versus CarD in vitro. The ability of the cognate CarDAd–CarGAd pair to interact, but not the noncognate CarDAd–CarG, rationalizes these data. Thus, in chimeras that conserve CarD–CarG interactions, the H1-like CTR of CarDAd could replace the CarD HMGA AT-hooks with no loss of function in vivo. More tellingly, even chimeras with the CarD AT-hook region substituted by human histone H1 CTR or full-length H1 functioned in M. xanthus. Our domain-swap analyses showing functional equivalence of HMGA AT-hooks and H1 CTR in prokaryotic transcriptional regulation provide molecular insights into possible modes of action underlying their biological roles.
Related Links	http://dx.doi.org/10.1073/pnas.0902233106
Ending Page	13551
Page Count	6
Starting Page	13546
File Format	PDF
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	32
Volume Number	106
Language	English
Publisher	National Academy of Sciences
Publisher Date	2009-08-11
Access Restriction	Open
Rights Holder	National Academy of Sciences
Subject Keyword	General Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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