Homework Help is Here – Start Your Trial Now!
Science
Biochemistry
Tryptophan synthase is one of the enzymes synthesized from the trp mRNA. In wild-type E. coli, the trp mRNA has a short half-life, but the tryptophan synthase half-life is much longer. To investigate how changes to the stability of the enzyme or its mRNA affect enzyme activity, two strains of E. coli were engineered. Strain A stabilizes the trp mRNA and strain B rapidly degrades tryptophan synthase. The wild-type, A, and B strains were grown in a medium with glucose as the sole carbon source. After several generations, tryptophan was added to all three cultures and tryptophan synthase activity was measured periodically. Note: Evaluate each condition as a simple model, where changes in the stability of trp mRNA or tryptophan synthase do not elicit secondary effects in the cells. Select the statements that describe the expected change in tryptophan synthase activity after the addition of tryptophan. In strain B, since both the trp mRNA and tryptophan synthase are rapidly degraded, the enzyme activity will drastically decrease. O In strain A, the trp mRNA is stable but the presence of tryptophan in the medium will cause the degradation of tryptophan synthase and abruptly decrease enzyme activity. O In the wild-type strain, the trp mRNA is degraded rapidly. However, since the tryptophan synthase is stable, the enzyme activity per cell will remain unchanged as the cells divide. In the wild-type strain, trp mRNA is unstable and will be degraded rapidly. As the cells continue to divide, tryptophan synthase will be diluted out and enzyme activity per cell will decrease. O In strain A, the trp mRNA will not be degraded and the cells will continue to synthesize tryptophan synthase. However, as the cells divide, the amount of enzyme activity per cell will slowly decrease.

Tryptophan synthase is one of the enzymes synthesized from the trp mRNA. In wild-type E. coli, the trp mRNA has a short half-life, but the tryptophan synthase half-life is much longer. To investigate how changes to the stability of the enzyme or its mRNA affect enzyme activity, two strains of E. coli were engineered. Strain A stabilizes the trp mRNA and strain B rapidly degrades tryptophan synthase. The wild-type, A, and B strains were grown in a medium with glucose as the sole carbon source. After several generations, tryptophan was added to all three cultures and tryptophan synthase activity was measured periodically. Note: Evaluate each condition as a simple model, where changes in the stability of trp mRNA or tryptophan synthase do not elicit secondary effects in the cells. Select the statements that describe the expected change in tryptophan synthase activity after the addition of tryptophan. In strain B, since both the trp mRNA and tryptophan synthase are rapidly degraded, the enzyme activity will drastically decrease. O In strain A, the trp mRNA is stable but the presence of tryptophan in the medium will cause the degradation of tryptophan synthase and abruptly decrease enzyme activity. O In the wild-type strain, the trp mRNA is degraded rapidly. However, since the tryptophan synthase is stable, the enzyme activity per cell will remain unchanged as the cells divide. In the wild-type strain, trp mRNA is unstable and will be degraded rapidly. As the cells continue to divide, tryptophan synthase will be diluted out and enzyme activity per cell will decrease. O In strain A, the trp mRNA will not be degraded and the cells will continue to synthesize tryptophan synthase. However, as the cells divide, the amount of enzyme activity per cell will slowly decrease.

Biochemistry
Biochemistry
9th Edition
ISBN:9781319114671
Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Chapter1: Biochemistry: An Evolving Science
Section: Chapter Questions
Problem 1P
See similar textbooks
icon
Related questions
Question
Tryptophan synthase is one of the enzymes synthesized from the trp mRNA. In wild-type E. coli, the trp mRNA has a short half-life, but the tryptophan synthase half-life is much longer. To investigate how changes to the stability of the enzyme or its mRNA affect enzyme activity, two strains of E. coli were engineered. Strain A stabilizes the trp mRNA and strain B rapidly degrades tryptophan synthase. The wild-type, A, and B strains were grown in a medium with glucose as the sole carbon source. After several generations, tryptophan was added to all three cultures and tryptophan synthase activity was measured periodically. Note: Evaluate each condition as a simple model, where changes in the stability of trp mRNA or tryptophan synthase do not elicit secondary effects in the cells. Select the statements that describe the expected change in tryptophan synthase activity after the addition of tryptophan. In strain B, since both the trp mRNA and tryptophan synthase are rapidly degraded, the enzyme activity will drastically decrease. In strain A, the trp mRNA is stable but the presence of tryptophan in the medium will cause the degradation of tryptophan synthase and abruptly decrease enzyme activity. O In the wild-type strain, the trp mRNA is degraded rapidly. However, since the tryptophan synthase is stable, the enzyme activity per cell will remain unchanged as the cells divide. O In the wild-type strain, trp mRNA is unstable and will be degraded rapidly. As the cells continue to divide, tryptophan synthase will be diluted out and enzyme activity per cell will decrease. In strain A, the trp mRNA will not be degraded and the cells will continue to synthesize tryptophan synthase. However, as the cells divide, the amount of enzyme activity per cell will slowly decrease.
Transcribed Image Text:Tryptophan synthase is one of the enzymes synthesized from the trp mRNA. In wild-type E. coli, the trp mRNA has a short half-life, but the tryptophan synthase half-life is much longer. To investigate how changes to the stability of the enzyme or its mRNA affect enzyme activity, two strains of E. coli were engineered. Strain A stabilizes the trp mRNA and strain B rapidly degrades tryptophan synthase. The wild-type, A, and B strains were grown in a medium with glucose as the sole carbon source. After several generations, tryptophan was added to all three cultures and tryptophan synthase activity was measured periodically. Note: Evaluate each condition as a simple model, where changes in the stability of trp mRNA or tryptophan synthase do not elicit secondary effects in the cells. Select the statements that describe the expected change in tryptophan synthase activity after the addition of tryptophan. In strain B, since both the trp mRNA and tryptophan synthase are rapidly degraded, the enzyme activity will drastically decrease. In strain A, the trp mRNA is stable but the presence of tryptophan in the medium will cause the degradation of tryptophan synthase and abruptly decrease enzyme activity. O In the wild-type strain, the trp mRNA is degraded rapidly. However, since the tryptophan synthase is stable, the enzyme activity per cell will remain unchanged as the cells divide. O In the wild-type strain, trp mRNA is unstable and will be degraded rapidly. As the cells continue to divide, tryptophan synthase will be diluted out and enzyme activity per cell will decrease. In strain A, the trp mRNA will not be degraded and the cells will continue to synthesize tryptophan synthase. However, as the cells divide, the amount of enzyme activity per cell will slowly decrease.
Expert Solution
trending now

Trending now

This is a popular solution!

steps

Step by step

Solved in 4 steps

SEE SOLUTIONCheck out a sample Q&A here
Blurred answer
Similar questions
  • SEE MORE QUESTIONS
Recommended textbooks for you
Biochemistry
Biochemistry
Biochemistry
ISBN:
9781319114671
Author:
Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Publisher:
W. H. Freeman
Lehninger Principles of Biochemistry
Lehninger Principles of Biochemistry
Biochemistry
ISBN:
9781464126116
Author:
David L. Nelson, Michael M. Cox
Publisher:
W. H. Freeman
Fundamentals of Biochemistry: Life at the Molecul…
Fundamentals of Biochemistry: Life at the Molecul…
Biochemistry
ISBN:
9781118918401
Author:
Donald Voet, Judith G. Voet, Charlotte W. Pratt
Publisher:
WILEY
Biochemistry
Biochemistry
Biochemistry
ISBN:
9781305961135
Author:
Mary K. Campbell, Shawn O. Farrell, Owen M. McDougal
Publisher:
Cengage Learning
Biochemistry
Biochemistry
Biochemistry
ISBN:
9781305577206
Author:
Reginald H. Garrett, Charles M. Grisham
Publisher:
Cengage Learning
Fundamentals of General, Organic, and Biological …
Fundamentals of General, Organic, and Biological …
Biochemistry
ISBN:
9780134015187
Author:
John E. McMurry, David S. Ballantine, Carl A. Hoeger, Virginia E. Peterson
Publisher:
PEARSON
SEE MORE TEXTBOOKS