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The function of e RF3 is to stimulate the activity of e RF1 through the hydrolysis of GTP (Zhouravleva et al., 1995), although the presence of e RF3 in human cells has been shown to be nonessential for termination (Le Goff et al., 1997).We also show that cell division in the fascicular cambial regions is altered, with the majority of vascular bundles containing cambial cells that are disorganized and possess enlarged nuclei.This is the first attempt at functional characterization of a release factor in vivo in plants and demonstrates the importance of e RF1-1 function in Arabidopsis.These plants primarily exhibit a reduction in internode elongation causing the formation of a broomhead-like cluster of malformed siliques at the top of the inflorescence stem.Histological analysis of stems revealed that cells are reduced in height and display ectopic lignification of the phloem cap cells, some phloem sieve cells, and regions of the fascicular cambium, as well as enhanced lignification of the interfascicular fibers.
Because e RF1 has a number of structural and functional similarities to a t RNA molecule, it has been hypothesized to enter the ribosomal A-site and catalyze the termination reaction through t RNA mimicry (Ito et al., 1996; Song et al., 2000).
Interaction between e RF1 and e RF3 C-terminal regions results in a conformational rearrangement of either e RF1 or both factors in the complex (Frolova et al., 1998).
Each stage requires specific accessory proteins or factors.
The signal that indicates the end of a polypeptide is the presence of an in-frame stop codon (UAA, UGA, or UAG) at the ribosomal A-site.
The role of the eukaryotic release factor 1 (e RF1) in translation termination has previously been established in yeast; however, only limited characterization has been performed on any plant homologs.
Here, we demonstrate that cosuppression of phenotype.