Anand, Kanchan

Czudnochowski, Nadine

Geyer, Matthias

Schulte, Antje

Vollmuth, Friederike

English

PubMed

Schulte Antje

Vollmuth Friederike

Czudnochowski Nadine

Anand Kanchan

Geyer Matthias

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Retrovirology

Insights into the activation of transcription elongation by lentiviruses: structure of the Cyclin T1-Tat-TAR RNA complex

Kanchan Anand

Nadine Czudnochowski

Friederike Vollmuth

Antje Schulte

Matthias Geyer

Springer - Publisher Connector

BioMed Central
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(page number not for citation purposes)
Retrovirology
Open AccessOral presentation
Insights into the activation of transcription elongation by 
lentiviruses: structure of the Cyclin T1-Tat-TAR RNA complex
Kanchan Anand1,2, Nadine Czudnochowski1, Friederike Vollmuth1, 
Antje Schulte1 and Matthias Geyer*1
Address: 1Max Planck Institute for Molecular Physiology, Dept. Physical Biochemistry, 44227 Dortmund, Germany and 2EMBL Heidelberg, 
Structural and Computational Biology Programme, 69117 Heidelberg, Germany
* Corresponding author    
The replication of many retroviruses is mediated by a tran-
scriptional activator protein, Tat, which activates RNA
polymerase II at the level of transcription elongation. Tat
interacts with Cyclin T1 of the positive transcription elon-
gation factor P-TEFb to recruit the transactivation-
response TAR RNA that acts as a promoter element in the
transcribed 5' end of the viral long terminal repeat. Here,
the structure of the cyclin box domain of CycT1 in com-
plex with the Tat protein from equine infections anemia
virus and its corresponding TAR RNA is presented. The
basic RNA recognition motif of Tat adopts a helical struc-
ture whose flanking regions interact with a cyclin T-spe-
cific loop in the first cyclin box repeat. Together both
proteins coordinate the stem-loop structure of TAR. Our
findings show that Tat binds to a similar surface on CycT1
as the recognition motifs from substrate and inhibitor
peptides were found to interact within Cdk/Cyclin pairs.
With the first insights into the structural basis of CycT1-
Tat-TAR recognition solved the rational identification of
specific target sites to interfere with the tripartite complex
assembly is becoming possible and the specificity for len-
tiviral vector systems apparent.
from Frontiers of Retrovirology: Complex retroviruses, retroelements and their hosts
Montpellier, France. 21-23 September 2009
Published: 24 September 2009
Retrovirology 2009, 6(Suppl 2):O18 doi:10.1186/1742-4690-6-S2-O18
<supplement> <title> <p>Frontiers of Retrovirology: Complex retroviruses, retroelements and their hosts</p> </title> <note>Meeting abstracts - A single PDF containing all abstracts in this Supplement is available <a href="http://www.biomedcentral.com/content/files/pdf/1742-4690-6-S2-full.pdf">here</a>.</note> <url>http://www.biomedcentral.com/content/pdf/1742-4690-6-S2-info.pdf</url> </supplement>
This abstract is available from: http://www.retrovirology.com/content/6/S2/O18
© 2009 Anand et al; licensee BioMed Central Ltd. 


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Insights into the activation of transcription elongation by lentiviruses: structure of the Cyclin T1-Tat-TAR RNA complex

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