Biochemistry: Concepts and Connections
Biochemistry: Concepts and Connections
1st Edition
ISBN: 9780321839923
Author: Dean R. Appling, Spencer J. Anthony-Cahill, Christopher K. Mathews
Publisher: PEARSON
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Chapter 26, Problem 12P
Interpretation Introduction

Interpretation:

Riboswitches are generally considered to have been discovered in about 2002. But a comparable regulatory process was described much earlier when Nomura et.al. Described the regulation of ribosomal protein synthesis carried out by binding of ribosomal proteins to their own mRNAs. Was the riboswitch actually discovered years earlier? Discuss similarities and differences in control of ribosomal protein synthesis and riboswitch regulation.

Concept Introduction:

Riboswitches are autoregulatory segments present in the mRNA that binds to specific molecules mainly the respective mRNA protein and control the protein synthesis from mRNA on which it resides. Riboswitches contain two regions aptamer and response platform upstream of the promoter of mRNA. The following diagram shows that binding of a small molecule to an aptamer, cause changes in response platform and make promoter unavailable for transcription.

    Biochemistry: Concepts and Connections, Chapter 26, Problem 12P

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Students have asked these similar questions
The beta-lactamase hydrolyzes the lactam-ring in penicillin. Describe the mechanism  of hydrolysis, insuring to include the involvement of S, D, & K in the reaction sequence. Please help
To map the active site of beta-lactamase, the enzyme was hydrolyzed with trypsin to yield a hexapeptide (P1) with the following amino acids. Glu, Lys, Leu, Phe, Met, and Ser. Treatment of P1 with phenyl isothiocyanate yielded a PTH derivative of phenylalanine and a peptide (P2). Treatment of P1 with cyanogenbromide gave an acidic tetrapeptide (P3) and a dipeptide (P4).Treatment of P2 with 1-fluoro-2,4-dinitrobenzene, followed by complete hydrolysis, yields N-2,4-dinitrophenyl-Glu. P1, P2, and P3 contain the active site serine. Why doesn't D in this hexapeptide not participate in the hydrolysis of the beta-lactam ring even though S, K, and D are involved in the catalyst?
To map the active site of -lactamase, the enzyme was hydrolyzed with trypsin to yield a hexapeptide (P1) with the following amino acids. Glu, Lys, Leu, Phe, Met, and Ser. Treatment of P1 with phenyl isothiocyanate yielded a PTH derivative of phenylalanine and a peptide (P2). Treatment of P1 with cyanogenbromide gave an acidic tetrapeptide (P3) and a dipeptide (P4).Treatment of P2 with 1-fluoro-2,4-dinitrobenzene, followed by complete hydrolysis, yields N-2,4-dinitrophenyl-Glu. P1, P2, and P3 contain the active site serine.  Using the experimental results described above derive the primary sequence of the active site hexapeptide. Please help!
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