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Full text of this paper is not available in the ETD Center. Copies may be available for inter-library loan from Kent State University or may be available for purchase from Proquest/UMI

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N-TERMINAL DOMAIN OF rRNA METHYLTRANSFERASE ENZYME RsmC IS IMPORTANT FOR ITS BINDING TO RNA AND RNA CHAPERON ACTIVITY

Kshetri, Man B.
http://orcid.org/0000-0002-4673-4662
http://rave.ohiolink.edu/etdc/view?acc_num=ksuhonors1621007414429417

Abstract Details

2021, BS, Kent State University, College of Arts and Sciences / Department of Chemistry and Biochemistry.
Ribosome is a ribonucleoprotein complex composed of three ribosomal RNAs and approximately 80 ribosomal proteins. It catalyzes the synthesis of proteins that regulate various biological processes in an organism, so proper ribosomal assembly is essential. In-vivo ribosomal biogenesis integrates number of processes, such as rRNA transcription, ribosome maturation, ribosome assembly, quality control, etc. It is speculated that r-proteins bind to rRNA co-transcriptionally along with other processes, such as nucleotide modification, rRNA folding, etc. Various rRNA modification enzymes also participate in ribosome biogenesis as assembly factor. More than 100 nucleotide modifications are distributed in various classes of RNAs in all kingdoms of life, but their functional role has not been discovered yet. In bacteria, 10 enzymes control 11 nucleotide modifications in 16s rRNA. Lack of those rRNA modifications result in growth defects, disease, and disorders by influencing ribosome assembly, but the direct link between nucleotide modification and ribosome assembly defects has not been determined yet. Ribosomal small subunit methyltransferase C (RsmC), a ribosomal RNA modification enzyme, catalyzes the transferring of methyl group from S-adenosyl methionine (SAM) to exocyclic amine of G1207 of 16S helix 34. It has two tandemly duplicated domain, methyltransferase active C-terminal domain and catalytically inert N-terminal domain. This project is focused on identifying the RNA strand that specifically binds to the N-terminal domain and also to evaluate the role of the RsmC N-terminal domain in the RNA chaperon activity. Various 16S helix 34 mutants are used to elucidate the biological role of RsmC under various conditions that generate ribosome mutations.
Sanjaya Abeysirigunawardena, Ph.D. (Advisor)
Yaorong Zheng, Ph.D. (Committee Member)
Xiaozhen Mou, Ph.D. (Committee Member)
Elda Hegmann, Ph.D. (Committee Member)
Biochemistry
RsmC, Ribosome, rRNA, Nucleotide modification, Protein, helix 34, ribosomal biogenesis

Recommended Citations

Citations

  • Kshetri, M. B. (2021). N-TERMINAL DOMAIN OF rRNA METHYLTRANSFERASE ENZYME RsmC IS IMPORTANT FOR ITS BINDING TO RNA AND RNA CHAPERON ACTIVITY [Undergraduate thesis, Kent State University]. OhioLINK Electronic Theses and Dissertations Center. http://rave.ohiolink.edu/etdc/view?acc_num=ksuhonors1621007414429417

    APA Style (7th edition)

  • Kshetri, Man. N-TERMINAL DOMAIN OF rRNA METHYLTRANSFERASE ENZYME RsmC IS IMPORTANT FOR ITS BINDING TO RNA AND RNA CHAPERON ACTIVITY. 2021. Kent State University, Undergraduate thesis. OhioLINK Electronic Theses and Dissertations Center, http://rave.ohiolink.edu/etdc/view?acc_num=ksuhonors1621007414429417.

    MLA Style (8th edition)

  • Kshetri, Man. "N-TERMINAL DOMAIN OF rRNA METHYLTRANSFERASE ENZYME RsmC IS IMPORTANT FOR ITS BINDING TO RNA AND RNA CHAPERON ACTIVITY." Undergraduate thesis, Kent State University, 2021. http://rave.ohiolink.edu/etdc/view?acc_num=ksuhonors1621007414429417

    Chicago Manual of Style (17th edition)

ksuhonors1621007414429417