Prescott's Microbiology
Prescott's Microbiology
10th Edition
ISBN: 9781259281594
Author: Joanne Willey, Linda Sherwood Adjunt Professor Lecturer, Christopher J. Woolverton Professor
Publisher: McGraw-Hill Education
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Chapter 5, Problem 5CHI
Summary Introduction

Generally, eukaryotic cells are larger than prokaryotic cells, such as bacteria and archaeal cells. Eukaryotes have complex structures and functions. They contain a nucleus and other membrane-bound organelles such as mitochondria, chloroplast, endoplasmic reticulum, Golgi apparatus, and lysosomes. Yeast, nematode worms, and mice are commonly used eukaryotic model organisms.

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Here we utilize a novel, well-characterized, endogenous mitochondrial mutation in the ATP6 gene of Drosophila melanogaster with a nearly complete loss of ATP synthase activity.  These Drosophila mutants have a missense mutation in ATP6 (G to A transition resulting in a glycine to glutamate change at position 116 in the protein), the mitochondrial gene encoding subunit 6 of the F1Fo-ATP synthase(complex V of the respiratory chain.  ATP6 allows for the hydrogen ion translocation required for the rotation of the Fo motor and the production of ATP from ADP. Drosophila ATP61 mutants model human mitochondrial encephalomyopathy and demonstrate phenotypes associated with degenerative disease, including: reduced longevity, mitochondrial pathology, progressive neural dysfunction, tissue degeneration and locomotor impairment.  ATP61 Drosophila mutants exhibit a stereotyped phenotypic progression that is analogous to the symptomatic progression reported for many human mitochondrial disease…
Researchers isolated a yeast phosphofructokinase (PFK) mutant in which a serine at the fructose-2,6-bisphosphate binding site was replaced with an aspartate residue. The amino acid substitution completely abolished the binding of fructose-2,6-bisphosphate to PFK. There was a dramatic decline in glucose consumption and ethanol production in the mutant compared to control yeast. Why can't the mutant PFK bind with fructose-2,6-bisphosphate?
Phosphofructokinase (PFK) catalyzes a key step in glycolysis. This enzyme is composed of three distinct subunits, muscle (M), liver (L) and platelet (P), which are expressed in different tissues. Mature human muscle contains exclusively the M isoform, while red blood cells express both M & L subunits. PFK gene mutations lead to M protein deficiency, intolerance to vigorous exercise and may lead to hemolytic anemia (Tarui disease). Which of the following can you conclude from the above information? Select all that apply. The muscle cells will be able to generate ATP through oxidative phosphorylation in the presence of oxygen U There may be a total lack of PFK activity in muscle O The red blood cells will be able to generate ATP through oxidative phosphorylation in the presence of oxygen U Hemolytic anemia may be due to instability of the L subunits in red blood cells
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Mitochondrial mutations; Author: Useful Genetics;https://www.youtube.com/watch?v=GvgXe-3RJeU;License: CC-BY