BIOLOGY
BIOLOGY
12th Edition
ISBN: 9781260169614
Author: Raven
Publisher: RENT MCG
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Chapter 10, Problem 1S

Regulation of the cell cycle is very complex and involves multiple proteins. In yeast, a complex of cdc2 and a mitotic cyclin is responsible for moving the cell past the G2/M checkpoint. The activity of the cyclin-dependent kinase cdc2 is inhibited when it is phosphorylated by the kinase, Wee-1. What would you predict would be the phenotype of a Wee-1 mutant yeast? What other genes could be altered in a Wee-1 deficient mutant strain that would make the cells act normally?

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Regulation of the cell cycle is very complex and involves multiple proteins. In yeast, a complex of cdc2 and a mitotic cyclin is responsible for moving the cell past the G2/M checkpoint. The activity of the cyclin-dependent kinase cdc2 is inhibited when it is phosphorylated by the kinase, Wee-1. What would you predict would be the phenotype of a Wee-1 mutant yeast? What other genes could be altered in a Wee-1 deficient mutant strain that would make the cells act normally?
The retinoblastoma protein (RB) suppresses human cell division by arresting cells in the G₁ phase of the cell cycle and preventing progression to the next phase. It accomplishes this task by binding to another protein, E2F, a transcription factor needed for further progression through the cell cycle. Normal progression through the cell cycle is accomplished when cyclin-dependent kinases (CDKs) phosphorylate RB, preventing its binding to E2F. Many viruses can induce abnormal exit from G, using viral proteins that bind to RB at a motif at the N-terminal called LXCXE. An example is the E7 papilloma protein, which causes the excessive proliferation of cells in warts. The site at which LXCXE proteins bind is called the pocket domain and is highly conserved on RB and related proteins in plants and animals. The configuration of the pocket domain is well established. Mutant experimental RB proteins are available with alterations in the conserved amino acids of the pocket domain. A simple…
The retinoblastoma protein (RB) suppresses human cell division by arresting cells in the G₁ phase of the cell cycle and preventing progression to the next phase. It accomplishes this task by binding to another protein, E2F, a transcription factor needed for further progression through the cell cycle. Normal progression through the cell cycle is accomplished when cyclin-dependent kinases (CDKs) phosphorylate RB, preventing its binding to E2F. Many viruses can induce abnormal exit from G, using viral proteins that bind to RB at a motif at the N-terminal called LXCXE. An example is the E7 papilloma protein, which causes the excessive proliferation of cells in warts. The site at which LXCXE proteins bind is called the pocket domain and is highly conserved on RB and related proteins in plants and animals. The configuration of the pocket domain is well established. Mutant experimental RB proteins are available with alterations in the conserved amino acids of the pocket domain. A simple…
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Mitochondrial mutations; Author: Useful Genetics;https://www.youtube.com/watch?v=GvgXe-3RJeU;License: CC-BY