Control of Messenger RNA Stability by Joel G. Belasco, George Brawerman

By Joel G. Belasco, George Brawerman

This can be the 1st finished overview of mRNA balance and its implications for law of gene expression. Written by way of specialists within the box, Control of Messenger RNA Stability serves either as a reference for experts in law of mRNA balance and as a basic creation for a broader neighborhood of scientists.

  • Provides views from either prokaryotic and eukaryotic systems
  • Offers a well timed, entire assessment of mRNA degradation, its rules, and its value within the keep an eye on of gene expression
  • Discusses the mechanisms, RNA structural determinants, and mobile components that keep an eye on mRNA degradation
  • Evaluates experimental techniques for learning mRNA degradation

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1985). Characterization of a cis-acting regulatory mutation that maps at the distal end of the Escherichia coli glyA gene. /. Bacteriol. 161, 650-654. Plamann, M. , and Stauffer, G. V. (1990). Escherichia coli glyA mRNA decay: The role of secondary structure and the effects of the pnp and rnb mutations. Mol. Gen. Genet. 220, 301-306. Portier, C. (1975). Quaternary structure of polynucleotide phosphorylase from Escherichia coli: Evidence of a complex between two types of polypeptide chains. Eur.

With this method, mRNA sequences from a specific region of a transcript would hybridize and give a positive signal, but no information could be gained as to the size of the hybridizing mRNA fragments and whether endonucleolytic cleavages had occurred in the particular region. The new method described by von Gabain et al. used uniformly labeled single-stranded DNA probes that were hybridized to RNA in solution and then subjected to S I nuclease digestion. The sizes of the complementary DNAs were different for upstream, middle, and downstream regions of the transcript.

Using gel retardation of labeled RNA as an assay, a protein with the appropriate characteristics has now been identified and partially characterized (H. C. Causton and C. F. Higgins, unpublished results). This protein binds to every stem-loop structure tested, irrespective of its sequence. In vitro, the partially purified protein impedes the progress of PNPase through stem-loop structures. Interestingly, this stem-loop binding protein copurifies with the catalytic subunit of PNPase. The possibility that it is the βsubunit of PNPase (which has not yet been assigned a function; see previous text) is attractive but remains to be tested.

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