Microbiology: An Evolving Science (Fourth Edition)
Microbiology: An Evolving Science (Fourth Edition)
4th Edition
ISBN: 9780393615098
Author: John W. Foster, Joan L. Slonczewski
Publisher: W. W. Norton & Company
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Chapter 13.3, Problem 2TQ
Summary Introduction

To review:

Formation of pyrophosphate (PPi) instead of inorganic phosphate (Pi) in a reaction, where hydrolysis of ATP (adenine triphosphate) is used to link amino acid to its cognate tRNA (transfer ribonucleic acid).

Introduction:

ATP can be used in three different manners to transfer energy to different cellular processes. At first, by hydrolysis which releases phosphate. In this, the hydrolysis of ATP produces ADP (adenine diphosphate) and Pi (inorganic phosphate). Secondly, by hydrolysis which releases pyrophosphate. In this, a pyrophosphate (PPi) is formed which ultimately breaks down into two molecules of Pi. In the third method an organic molecule is phosphorylated.

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Many blood clotting proteins undergo a post-translational modification in which specific glutamic acid residues (Glu) in the protein are converted to gamma-carboxyglutamic acid residues (Gla). See reaction scheme below. An example is the blood clotting protein Factor IX, which has 12 Glu in its N-terminus converted to Gla. This modification gives Factor IX the ability to bind calcium and phospholipid membranes. Bacteria do not have the enzyme required to convert Glu to Gla and therefore Factor IX proteins expressed in bacteria would not have the proper modifications. How might you engineer the translational apparatus of a bacterial cell line so that it produces Factor IX with Gla in the appropriate positions. How would you ensure that only the 12 Glu in Factor IX that are normally converted to Gla and not just all Glu (Limit 5-6 senetnces)?
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