Evidence map›Paper›PMID 21673140›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2011

Structural basis for recognition of AT-rich DNA by unrelated xenogeneic silencing proteins.

Blair R G Gordon, Yifei Li, Atina Cote, Matthew T Weirauch, Pengfei Ding, Timothy R Hughes, William Wiley Navarre, Bin Xia, Jun Liu

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 140 papers.

0numbers the graph read from it
0cells of the map it votes in
140citing papers in PubMed
8.8field-weighted citation impact, top 2% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

140 citing papers in PubMed, 248 citations in OpenAlex.

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80 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

9 authors at 2 institutions in 2 countries.

Blair R G GordonDepartment of Molecular Genetics, University of Toronto, Toronto, ON, Canada M5S 1A8.
Yifei Li
Atina Cote
Matthew T Weirauch
Pengfei Ding
Timothy R Hughes
William Wiley Navarre
Bin Xia
Jun Liu
University of Toronto · CAPeking University · CN

Funding

Canadian Institutes of Health Research MOP-15107Canadian Institutes of Health Research MOP-77721Canadian Institutes of Health Research MOP-86683
6 · The paper itself

Abstract

H-NS and Lsr2 are nucleoid-associated proteins from Gram-negative bacteria and Mycobacteria, respectively, that play an important role in the silencing of horizontally acquired foreign DNA that is more AT-rich than the resident genome. Despite the fact that Lsr2 and H-NS proteins are dissimilar in sequence and structure, they serve apparently similar functions and can functionally complement one another. The mechanism by which these xenogeneic silencers selectively target AT-rich DNA has been enigmatic. We performed high-resolution protein binding microarray analysis to simultaneously assess the binding preference of H-NS and Lsr2 for all possible 8-base sequences. Concurrently, we performed a detailed structure-function relationship analysis of their C-terminal DNA binding domains by NMR. Unexpectedly, we found that H-NS and Lsr2 use a common DNA binding mechanism where a short loop containing a "Q/RGR" motif selectively interacts with the DNA minor groove, where the highest affinity is for AT-rich sequences that lack A-tracts. Mutations of the Q/RGR motif abolished DNA binding activity. Netropsin, a DNA minor groove-binding molecule effectively outcompeted H-NS and Lsr2 for binding to AT-rich sequences. These results provide a unified molecular mechanism to explain findings related to xenogeneic silencing proteins, including their lack of apparent sequence specificity but preference for AT-rich sequences. Our findings also suggest that structural information contained within the DNA minor groove is deciphered by xenogeneic silencing proteins to distinguish genetic material that is self from nonself.

Indexed as

AT Rich SequenceNucleic Acid ConformationAmino Acid SequenceBacterial ProteinsBase SequenceDNADNA-Binding ProteinsModels, MolecularMolecular Sequence DataNuclear Magnetic Resonance, BiomolecularSequence Homology, Amino AcidBacterial ProteinsDNADNA-Binding ProteinsH-NS protein, bacteria

Identifiers

PMID21673140
PMCPMC3127928
OpenAlexW2096926750

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.