Use this URL to cite or link to this record in EThOS: http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.419647
Title: Characterisation of the localisation of histone hairpin binding protein and its role in translation of histone mRNA
Author: Andrews, Stuart Christopher
Awarding Body: University of Aberdeen
Current Institution: University of Aberdeen
Date of Award: 2005
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Abstract:
Histones are proteins required for packaging of DNA in the nucleus.  Metazoan replication-dependent histone genes are expressed only during S-phase, intronless, and their mRNAs do not end in a poly(A) tail but rather a highly conserved hairpin structure.  Hairpin binding protein (HBP or Stem-Loop Binding Protein) specifically binds to the hairpin structure of histone pre-mRNA.  This interaction is important during the endonucleolytic cleavage reaction to generate the mature histone mRNA.  I have performed preliminary work to identify nucleotides in the hairpin structure that are involved in the interaction with HBP. HBP expression occurs concurrently with expression of histone genes during S-phase.  A hairpin RNA binding activity, presumed to be HBP has been previously demonstrated in both nuclear and cytoplasmic extracts.  I have used a specific antibody to show that hHBP has a histone RNA-independent localisation in both the nucleus and cytoplasm only during S-phase.  Also, I have examined the localisation of an exclusively nuclear alternative splice variant of HBP which arises from skipping of exon 3 of mouse and human HBP mRNA. Efficient translation of histone mRNA is dependent on HBP.  I show that a minor fraction of cytoplasmic hHBP associates with ribosomes in an RNA-dependent manner and show that HBP stimulates translation.  I further participated in mapping of the HBP region required for the translation stimulation by a motif encoded by xSLBP1 exon 3 found in xSLBP1-Nt and characterised interactions between HBP and translation initiation factors, eIF3h and PAIP1, mediated by hHBP RBD and Ct, respectively.
Supervisor: Not available Sponsor: Not available
Qualification Name: Thesis (Ph.D.) Qualification Level: Doctoral
EThOS ID: uk.bl.ethos.419647  DOI: Not available
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