schliessen

Filtern

 

Bibliotheken

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

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 s... Full description

Journal Title: Proceedings of the National Academy of Sciences of the United States of America June 28, 2011, Vol.108(26), pp.10690-10695
Main Author: Gordon, Blair R G
Other Authors: Li, Yifei , Cote, Atina , Weirauch, Matthew T , Ding, Pengfei , Hughes, Timothy R , Navarre, William Wiley , Xia, Bin , Liu, Jun
Format: Electronic Article Electronic Article
Language: English
Subjects:
DNA
ID: E-ISSN: 1091-6490 ; DOI: 10.1073/pnas.1102544108
Link: http://search.proquest.com/docview/874296108/?pq-origsite=primo
Zum Text:
SendSend as email Add to Book BagAdd to Book Bag
Staff View
recordid: proquest874296108
title: Structural basis for recognition of AT-rich DNA by unrelated xenogeneic silencing proteins.
format: Article
creator:
  • Gordon, Blair R G
  • Li, Yifei
  • Cote, Atina
  • Weirauch, Matthew T
  • Ding, Pengfei
  • Hughes, Timothy R
  • Navarre, William Wiley
  • Xia, Bin
  • Liu, Jun
subjects:
  • At Rich Sequence–Chemistry
  • Amino Acid Sequence–Metabolism
  • Bacterial Proteins–Chemistry
  • Base Sequence–Metabolism
  • DNA–Chemistry
  • DNA-Binding Proteins–Metabolism
  • Models, Molecular–Metabolism
  • Molecular Sequence Data–Metabolism
  • Nuclear Magnetic Resonance, Biomolecular–Metabolism
  • Nucleic Acid Conformation–Metabolism
  • Sequence Homology, Amino Acid–Metabolism
  • Bacterial Proteins
  • DNA-Binding Proteins
  • H-Ns Protein, Bacteria
  • DNA
ispartof: Proceedings of the National Academy of Sciences of the United States of America, June 28, 2011, Vol.108(26), pp.10690-10695
description: 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. doi/ 10.1073/pnas.1102544108
language: eng
source:
identifier: E-ISSN: 1091-6490 ; DOI: 10.1073/pnas.1102544108
fulltext: fulltext
issn:
  • 10916490
  • 1091-6490
url: Link


@attributes
ID76065705
RANK0.07
NO1
SEARCH_ENGINEprimo_central_multiple_fe
SEARCH_ENGINE_TYPEPrimo Central Search Engine
LOCALfalse
PrimoNMBib
record
control
sourcerecordid874296108
sourceidproquest
recordidTN_proquest874296108
sourcesystemPC
pqid874296108
galeid261318527
display
typearticle
titleStructural basis for recognition of AT-rich DNA by unrelated xenogeneic silencing proteins.
creatorGordon, Blair R G ; Li, Yifei ; Cote, Atina ; Weirauch, Matthew T ; Ding, Pengfei ; Hughes, Timothy R ; Navarre, William Wiley ; Xia, Bin ; Liu, Jun
contributorGordon, Blair R G (correspondence author) ; Gordon, Blair R G (record owner)
ispartofProceedings of the National Academy of Sciences of the United States of America, June 28, 2011, Vol.108(26), pp.10690-10695
identifierE-ISSN: 1091-6490 ; DOI: 10.1073/pnas.1102544108
subjectAt Rich Sequence–Chemistry ; Amino Acid Sequence–Metabolism ; Bacterial Proteins–Chemistry ; Base Sequence–Metabolism ; DNA–Chemistry ; DNA-Binding Proteins–Metabolism ; Models, Molecular–Metabolism ; Molecular Sequence Data–Metabolism ; Nuclear Magnetic Resonance, Biomolecular–Metabolism ; Nucleic Acid Conformation–Metabolism ; Sequence Homology, Amino Acid–Metabolism ; Bacterial Proteins ; DNA-Binding Proteins ; H-Ns Protein, Bacteria ; DNA
languageeng
source
descriptionH-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. doi/ 10.1073/pnas.1102544108
version10
lds50peer_reviewed
links
openurl$$Topenurl_article
openurlfulltext$$Topenurlfull_article
backlink$$Uhttp://search.proquest.com/docview/874296108/?pq-origsite=primo$$EView_record_in_ProQuest_(subscribers_only)
search
creatorcontrib
0Gordon, Blair R G
1Li, Yifei
2Cote, Atina
3Weirauch, Matthew T
4Ding, Pengfei
5Hughes, Timothy R
6Navarre, William Wiley
7Xia, Bin
8Liu, Jun
titleStructural basis for recognition of AT-rich DNA by unrelated xenogeneic silencing proteins.
subject
0At Rich Sequence–Chemistry
1Amino Acid Sequence–Metabolism
2Bacterial Proteins–Chemistry
3Base Sequence–Metabolism
4DNA–Chemistry
5DNA-Binding Proteins–Metabolism
6Models, Molecular–Metabolism
7Molecular Sequence Data–Metabolism
8Nuclear Magnetic Resonance, Biomolecular–Metabolism
9Nucleic Acid Conformation–Metabolism
10Sequence Homology, Amino Acid–Metabolism
11Bacterial Proteins
12DNA-Binding Proteins
13H-Ns Protein, Bacteria
14DNA
152L92
162L93
17PDB
general
0English
110.1073/pnas.1102544108
2MEDLINE (ProQuest)
3ProQuest Biological Science Collection
4ProQuest Natural Science Collection
5ProQuest SciTech Collection
6Biological Science Database
7Natural Science Collection
8SciTech Premium Collection
9Health Research Premium Collection
10Health Research Premium Collection (Alumni edition)
11Biological Science Index (ProQuest)
sourceidproquest
recordidproquest874296108
issn
010916490
11091-6490
rsrctypearticle
creationdate2011
addtitleProceedings of the National Academy of Sciences of the United States of America
searchscope
01007527
11007944
21009130
310000004
410000038
510000050
610000120
710000159
810000238
910000253
1010000260
1110000270
1210000271
1310000302
1410000350
15proquest
scope
01007527
11007944
21009130
310000004
410000038
510000050
610000120
710000159
810000238
910000253
1010000260
1110000270
1210000271
1310000302
1410000350
15proquest
lsr43
01007527false
11007944false
21009130false
310000004false
410000038false
510000050false
610000120false
710000159false
810000238false
910000253false
1010000260false
1110000270false
1210000271false
1310000302false
1410000350false
contributorGordon, Blair R G
startdate20110628
enddate20110628
citationpf 10690 pt 10695 vol 108 issue 26
lsr30VSR-Enriched:[description, issn, pqid, galeid]
sort
titleStructural basis for recognition of AT-rich DNA by unrelated xenogeneic silencing proteins.
authorGordon, Blair R G ; Li, Yifei ; Cote, Atina ; Weirauch, Matthew T ; Ding, Pengfei ; Hughes, Timothy R ; Navarre, William Wiley ; Xia, Bin ; Liu, Jun
creationdate20110628
lso0120110628
facets
frbrgroupid7729410986199212009
frbrtype5
newrecords20181218
languageeng
creationdate2011
topic
0At Rich Sequence–Chemistry
1Amino Acid Sequence–Metabolism
2Bacterial Proteins–Chemistry
3Base Sequence–Metabolism
4DNA–Chemistry
5DNA-Binding Proteins–Metabolism
6Models, Molecular–Metabolism
7Molecular Sequence Data–Metabolism
8Nuclear Magnetic Resonance, Biomolecular–Metabolism
9Nucleic Acid Conformation–Metabolism
10Sequence Homology, Amino Acid–Metabolism
11Bacterial Proteins
12DNA-Binding Proteins
13H-Ns Protein, Bacteria
14DNA
collection
0MEDLINE (ProQuest)
1ProQuest Biological Science Collection
2ProQuest Natural Science Collection
3ProQuest SciTech Collection
4Biological Science Database
5Natural Science Collection
6SciTech Premium Collection
7Health Research Premium Collection
8Health Research Premium Collection (Alumni edition)
9Biological Science Index (ProQuest)
prefilterarticles
rsrctypearticles
creatorcontrib
0Gordon, Blair R G
1Li, Yifei
2Cote, Atina
3Weirauch, Matthew T
4Ding, Pengfei
5Hughes, Timothy R
6Navarre, William Wiley
7Xia, Bin
8Liu, Jun
jtitleProceedings of the National Academy of Sciences of the United States of America
toplevelpeer_reviewed
delivery
delcategoryRemote Search Resource
fulltextfulltext
addata
aulast
0Gordon
1Li
2Cote
3Weirauch
4Ding
5Hughes
6Navarre
7Xia
8Liu
aufirst
0Blair R G
1Yifei
2Atina
3Matthew T
4Pengfei
5Timothy R
6William Wiley
7Bin
8Jun
au
0Gordon, Blair R G
1Li, Yifei
2Cote, Atina
3Weirauch, Matthew T
4Ding, Pengfei
5Hughes, Timothy R
6Navarre, William Wiley
7Xia, Bin
8Liu, Jun
addauGordon, Blair R G
atitleStructural basis for recognition of AT-rich DNA by unrelated xenogeneic silencing proteins.
jtitleProceedings of the National Academy of Sciences of the United States of America
risdate20110628
volume108
issue26
spage10690
epage10695
pages10690-10695
eissn1091-6490
formatjournal
genrearticle
ristypeJOUR
doi10.1073/pnas.1102544108
urlhttp://search.proquest.com/docview/874296108/
issn00278424
date2011-06-28