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Learning about the structure of the CRO Repressorprotein

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Introduction

Learning about the structure of the CRO Repressor protein As we all know; a proteins structure can be found in the cell wall in a bacteria or a membrane of eukayrotic, extracellular matrise. They function as enzymes or catalysts to either speed up or slow down a chemical reaction. These proteins produce antibodies within the cell immune system for protection against harmful cells. Other functions include the transport and storage of protein molecules and also control the growth and differentiation. ...read more.

Middle

* C-terminal domain: the domain mediates dimerization. 434 Cro protein - a single domain protein with a homologous structure to R1-69. Helices 4 and 5 provide part of the dimer interface. Proteins bind to 6 related operator sites (named OL1-3 and OR1-3) with varying affinities. Each site is 14 bp with 4-conserved bp at either end. The central 6 bp modulate protein-binding affinity. Helix 3 makes base contacts in the major groove while helix 2 and the helix 2/3 turn bind the DNA backbone. ...read more.

Conclusion

A competition between the cro and repressor proteins ensues, the outcome of which determines whether the phage embarks on a lytic or lysogenic lifecycle. Cro and repressor compete for control of an operator region containing three operators that determine the state of the lytic/lysogenic genetic switch. If repressor wins this competition, transcription of the cro gene is blocked and repressor synthesis is maintained. Lysogeny will result. A competition won by cro, however, means that the late genes of phage l will be expressed; this will result in lysis. In this case, cro blocks transcription that occurs from Prm, the promoter that is responsible for the maintenance of repressor transcription. Khabil Miah CRO Repressor Protein ...read more.

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