ISSN:
1573-9023
Keywords:
Tat
;
TAR
;
RNA binding proteins
;
Arginine-rich domains
;
Transcriptional activators
;
Activation domains
;
RNA conformational changes
;
RNA bulges
;
Electrostatic interactions
;
Cooperativity
;
Kinetic vs thermodynamic stability
Source:
Springer Online Journal Archives 1860-2000
Topics:
Chemistry and Pharmacology
Notes:
Summary The HIV Tat protein effects potent transcriptional activation of viral long terminal repeat-linked genes subsequent to binding an RNA target structure, termed TAR. Sequence-specific interactions, structure-specific electrostatic interactions, and cooperation with facilitating (cellular) factors collaborate for productive targeting. Binding occurs at a simple bulge loop, a ubiquitous element of RNA structure, and is mediated, in part, by an arginine-rich subdomain, found in many proteins that bind RNA. Principles elucidated from the Tat-TAR interaction provide a model for diverse RNA-protein interactions.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1007/BF02171664
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