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Genetic and Biochemical Analysis of the Spliceosomal GTPase Snu114

Tamara J. Brenner

出版	University of California, San Francisco, 2005
ISBN	05424603789780542460371
URL	http://books.google.com.hk/books?id=qT2se1rR7yYC&hl=&source=gbs_api

註釋

A second class of SNU114 mutations greatly reduces the formation of the U5 snRNP and U5•U4/U6 tri-snRNPs. In these mutants, the interaction between Snu114 and Prp8 is reduced, and the total levels of Prp8 are decreased. These mutations fall within conserved motifs in the GTPase domain and in small clusters within each of domains III-V. We predict that these mutations either directly affect GTP binding/hydrolysis, or impact a rearrangement of the protein resulting from changes in nucleotide binding. We propose that Snu114 must bind GTP in order to interact productively with Prp8 and that this GTP-bound heterodimer is required in turn to assemble the U5 snRNP. This strategy would ensure that Snu114 is bound to GTP when it joins the spliceosome; subsequent GTP hydrolysis would then lead to spliceosome activation.