Abstract
dc:description.abstractThe goal of the project was to determine the crystal structure of TB-RBP (Testis/Brain RNA binding protein) in complex with single stranded DNA. The secondary goal was to determine the crystal structure of TB-RBP in complex with Trax (translin associated factor X). Functions of TB-RBP is to suppresses translation of testicular mRNAs (Ex: protamines 1 and 2), attach mRNAs to microtubules for cellular transport of brain mRNAs and to mediate both temporal and spatial expression of certain mRNAs in male germ cell development. Translin is the human homologue of mouse TB-RBP. Translin is proposed to function as a DNA-binding protein that binds to specific DNA sequences at breakpoint junctions of chromosomal translocations of lymphoid malignancies. Trax, structural homologue of TB-RBP, has already been shown to interact with the single stranded DNA -/RNA - binding protein TB-RBP. Co-crystallization of TB-RBP/DNA complex may give us insight into sequence recognition at the breakpoint junctions of chromosomal translocation. Co-crystallization of a Trax/TB-RBP complex may provide insight into regulation of silenced mRNA.
Author and committee
dc:creator, dc:contributor.*- Author dc:creator
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- Hoe, Warren
- Contributors dc:contributor
-
- Robertus, Jon D.
Subjects
dc:subject × 3Rights
dc:rights- Statement dc:rights
-
- Restricted
- Copyright © is held by the author. Presentation of this material on the Libraries' web site by University Libraries, The University of Texas at Austin was made possible under a limited license grant from the author who has retained all copyrights in the works.
- Language dc:language
- eng
Identifiers
dc:identifier.*- Identifier
- http://dx.doi.org/10.26153/tsw/4520
- OAI identifier oai:identifier
- oai:tdl-ir.tdl.org:2152/77431