Research Paper on Validation of the RNA Polymerase Omega Subunit as a Functional Entity

Description

Title: Validation of the RNA Polymerase Omega Subunit as a Functional Entity

Abstract: The multi-subunit protein complex (2′ ) known as the bacterial RNA polymerase (RNAP) contains the smallest subunit,. Although it was discovered early on in RNAP research, its purpose was unclear and surrounded by debate for a long time. It has been established that the protein plays a structural part in preserving the largest subunit’s conformation and recruiting it to the enzyme assembly. Despite’s function in the assembly of RNAP and its evolutionary conservation, E. The global chaperone protein GroEL is associated with RNAP, allowing rpoZ-deficient coli mutants to survive. Several dominant lethal mutants of were isolated in order to gain more understanding of the structure and functional role of during transcription. When compared to native, the mutants’ binding affinity to the 2′ subassembly was higher. We found that a small but unfavorable negative entropy term and mostly favorable enthalpy drive the interaction between 2′ and these lethal mutants. But accidentally, while isolating these mutants, we also managed to isolate a silent mutant with a lethal phenotype. The definition of a silent mutant of a given protein is a protein with the same amino acid sequence as the wild type but a gene mutation caused by codon degeneracy that changes the base sequence from a more frequent code to a less frequent one. To finally comprehend the function of rare codons at various positions in rpoZ, a large number of silent mutants were created. We noticed that the dominant lethal mutants of that are either silent or point mutations are more structured than the native. However, the position of the silent code in the rpoZ reading frame affects the structural modification to the protein that was translated. The rigidity of this structural change in affects the plasticity of the interacting domain formed by and 2′. Here, we tried to explain how the conformational flexibility of the contributes to preserving the plasticity of the RNA polymerase active site. The suppressor for both types of dominant lethal mutants of is located close to the catalytic center of the’subunit.

Keywords: ω-subunit; RNA polymerase; structure; silent mutants; plasticity

Paper Quality: SCOPUS / Web of Science Level Research Paper

Subject: Biomolecules

Writer Experience: 20+ Years

Plagiarism Report: Turnitin Plagiarism Report will be less than 10%

Restriction: Only one author may purchase a single paper. The paper will then indicate that it is out of stock.

What will I get after the purchase?

A turnitin plagiarism report of less than 10% in a pdf file and a full research paper in a word document.

In case you have any questions related to this research paper, please feel free to call/ WhatsApp on +919726999915