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  Case in Point : Complete Case Interview Preparation. Ninth edition.

  Marc P. Cosentino.

  Summary: "Cosentino demystifies the consulting case interview. He takes you inside a typical interview by exploring the various types of case questions and he shares with you a system that will help you answer today's most sophisticated case questions"--Page 4 of cover.
  
  Contents:
  The interview
  Case questions
  Ivy Case System
  Practice cases
  Case starts
  Partner cases
  Final analysis
  Partner case charts.

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  BioSciences Career Center Collection (Duck Room)

  [2016]

  Consult 102

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• Article

  An Escherichia coli ribonuclease which removes an extra nucleotide from a biosynthetic intermediate of bacteriophage T4 proline transfer RNA.

  Schmidt FJ, McClain WH.

  Nucleic Acids Res. 1978 Nov;5(11):4129-39.

  The biosynthesis of bacteriophage T4 tRNAPro, tRNASer, and tRNAIle requires enzymatic removal of extra nucleotides from the 3' terminus of the respective precursor RNAs. A ribonuclease activity capable of catalyzing such reactions has been partially purified from uninfected Escherichia coli using an artificial precursor RNA as substrate. A number of ribonuclease activities were resolved during purification. Use of E. coli strain BN, a mutant known to be deficient in the relevant ribonuclease activity, permitted us to identify it in wild-type cells. This activity was designated the BN ribonuclease. BN ribonuclease had an apparent molecular weight of 35,000 as measured by Sephadex gel filtration. Mg2+ was required for activity, which was optimal at [Mg2+] of 2mM. Activity did not require monovalent cations K+ or Na+. BN ribonuclease was less efficient at removing extra residues in the biosynthesis of tRNASer and tRNAIle than in the biosynthesis of tRNAPro.

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  PubMed