PMID- 21166891
OWN - NLM
STAT- MEDLINE
DCOM- 20110406
LR  - 20220129
IS  - 1365-2958 (Electronic)
IS  - 0950-382X (Print)
IS  - 0950-382X (Linking)
VI  - 79
IP  - 1
DP  - 2011 Jan
TI  - Association of OLE RNA with bacterial membranes via an RNA-protein interaction.
PG  - 21-34
LID - 10.1111/j.1365-2958.2010.07439.x [doi]
AB  - Ornate, large, extremophilic (OLE) RNAs are large, non-coding transcripts 
      characterized by their ornate secondary structure and presence predominantly in 
      Gram-positive, extremophilic bacteria. A gene for an OLE-associated protein (OAP) 
      is almost always located immediately downstream of the OLE gene. OAP has no 
      extensive homology to other proteins and is predicted to form multiple 
      transmembrane domains. We show that this protein forms a ribonucleoprotein 
      complex with OLE RNA using at least 2:1 protein : RNA stoichiometry. A series of 
      truncated OLE RNA constructs was used to establish that most of the RNA can be 
      deleted without eliminating protein binding. Two primary binding sites are 
      present within the RNA, although additional binding determinants exist and 
      extensive structural stabilization is induced by OAP. RNA fluorescence in situ 
      hybridization (FISH) was used in Escherichia coli to demonstrate that 
      ribonucleoprotein complex formation localizes the RNA near cell membranes of this 
      heterologous system. Therefore, the majority of the complex structure formed by 
      OLE RNA may perform a biochemical function that requires membrane localization.
CI  - (c) 2010 Blackwell Publishing Ltd.
FAU - Block, Kirsten F
AU  - Block KF
AD  - Department of Molecular, Cellular and Developmental Biology, Yale University, New 
      Haven, CT 06520, USA.
FAU - Puerta-Fernandez, Elena
AU  - Puerta-Fernandez E
FAU - Wallace, Jason G
AU  - Wallace JG
FAU - Breaker, Ronald R
AU  - Breaker RR
LA  - eng
GR  - HHMI/Howard Hughes Medical Institute/United States
GR  - P01 GM022778/GM/NIGMS NIH HHS/United States
GR  - P01 GM022778-24/GM/NIGMS NIH HHS/United States
PT  - Journal Article
DEP - 20101116
PL  - England
TA  - Mol Microbiol
JT  - Molecular microbiology
JID - 8712028
RN  - 0 (Bacterial Proteins)
RN  - 0 (RNA, Bacterial)
RN  - 0 (RNA, Untranslated)
RN  - 0 (Ribonucleoproteins)
SB  - IM
CIN - Mol Microbiol. 2011 Jan;79(1):1-2. PMID: 21210530
MH  - Bacteria, Anaerobic/chemistry/genetics/*metabolism
MH  - Bacterial Proteins/chemistry/genetics/*metabolism
MH  - Binding Sites
MH  - Cell Membrane/chemistry/genetics/*metabolism
MH  - Cloning, Molecular
MH  - Escherichia coli/chemistry/genetics
MH  - Gene Expression
MH  - Models, Molecular
MH  - Nucleic Acid Conformation
MH  - Protein Binding
MH  - RNA, Bacterial/chemistry/genetics/metabolism
MH  - RNA, Untranslated/chemistry/genetics/*metabolism
MH  - Ribonucleoproteins/chemistry/*metabolism
MH  - Sequence Deletion
PMC - PMC3552494
MID - NIHMS265554
EDAT- 2010/12/21 06:00
MHDA- 2011/04/07 06:00
PMCR- 2013/01/23
CRDT- 2010/12/21 06:00
PHST- 2010/12/21 06:00 [entrez]
PHST- 2010/12/21 06:00 [pubmed]
PHST- 2011/04/07 06:00 [medline]
PHST- 2013/01/23 00:00 [pmc-release]
AID - 10.1111/j.1365-2958.2010.07439.x [doi]
PST - ppublish
SO  - Mol Microbiol. 2011 Jan;79(1):21-34. doi: 10.1111/j.1365-2958.2010.07439.x. Epub 
      2010 Nov 16.