PMID- 21663314
OWN - NLM
STAT- MEDLINE
DCOM- 20111010
LR  - 20110712
IS  - 1520-4995 (Electronic)
IS  - 0006-2960 (Linking)
VI  - 50
IP  - 28
DP  - 2011 Jul 19
TI  - Structure of the HIV-1 5' untranslated region dimer alone and in complex with 
      gold nanocolloids: support of a TAR-TAR-containing 5' dimer linkage site (DLS) 
      and a 3' DIS-DIS-containing DLS.
PG  - 6170-7
LID - 10.1021/bi200488h [doi]
AB  - The formation of a genomic RNA dimer is critical for the HIV-1 replication cycle, 
      and dimerization is known to initiate within the 5'UTR (5' untranslated region) 
      of the viral RNA. However, the 5'UTR constitutes the 335 terminal nucleotides, 
      and because of this considerable size, it has been difficult to study the global 
      structure using conventional structural methods. Here, the atomic force 
      microscope has been used to directly visualize the dimer formed from RNAs 
      including HIV-1 nucleotides 1-744. Gold nanocolloids were deposited on the primer 
      binding site regions in the dimer as an internal control. The dimer showed 
      distinct ring morphology with up to two gold nanocolloids deposited within the 
      ring and one or two strands extending from the ring. This morphology implies a 
      dimer including a DIS-DIS (dimerization initiation site)-containing 3' dimer 
      linkage site (DLS) and a TAR-TAR (trans-activation region)-containing 5'DLS. 
      Furthermore, the dimer was formed under the influence of Mg(2+) and was imaged 
      with an atomic force microscope under buffer conditions. The overall ring 
      morphology containing a 5'DLS and a 3'DLS with one or two strands extending from 
      it was conserved in these atomic force microscopy images. This indicates that the 
      observed dimer morphology is physiologically significant. Moreover, evidence of 
      multiple dimer interstrand contacts downstream of the major splice donor were 
      observed, which indicates a component in the selection of full-length genomic RNA 
      in dimer formation during virion packaging.
FAU - Pallesen, Jesper
AU  - Pallesen J
AD  - Department of Biochemistry and Molecular Biophysics, Howard Hughes Medical 
      Institute, Columbia University, New York, New York 10032, United States. 
      jp2854@columbia.edu
LA  - eng
GR  - Howard Hughes Medical Institute/United States
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
DEP - 20110622
PL  - United States
TA  - Biochemistry
JT  - Biochemistry
JID - 0370623
RN  - 0 (3' Untranslated Regions)
RN  - 0 (5' Untranslated Regions)
RN  - 0 (Colloids)
RN  - 0 (RNA, Viral)
RN  - 0 (RNA-Binding Proteins)
RN  - 136628-24-5 (trans-activation responsive RNA-binding protein)
RN  - 7440-57-5 (Gold)
SB  - IM
MH  - *3' Untranslated Regions
MH  - *5' Untranslated Regions
MH  - Base Sequence
MH  - Colloids/*chemistry
MH  - Gold/*chemistry
MH  - HIV-1/*chemistry/physiology
MH  - Microscopy, Atomic Force
MH  - Nanostructures/chemistry
MH  - Nucleic Acid Conformation
MH  - *Protein Multimerization
MH  - RNA Splicing/genetics
MH  - RNA, Viral/*chemistry/metabolism
MH  - RNA-Binding Proteins/*chemistry/genetics/metabolism
MH  - Virus Activation
MH  - Virus Replication
EDAT- 2011/06/15 06:00
MHDA- 2011/10/11 06:00
CRDT- 2011/06/14 06:00
PHST- 2011/06/14 06:00 [entrez]
PHST- 2011/06/15 06:00 [pubmed]
PHST- 2011/10/11 06:00 [medline]
AID - 10.1021/bi200488h [doi]
PST - ppublish
SO  - Biochemistry. 2011 Jul 19;50(28):6170-7. doi: 10.1021/bi200488h. Epub 2011 Jun 
      22.