Item Details

title

INVESTIGATING FUNCTIONAL HETEROGENEITY IN RIBOSOMAL PROTEIN PARALOGS IN SCHIZOSACCHAROMYCES POMBE

author

VonRuden, Dalton

abstract

Ribosomes are more heterogeneous than previously thought, with heterogeneitypotentially resulting in ribosomes capable of specialized functions. I focus on Rpl2701 and Rpl2702, large ribosomal subunit 27 (Rpl27) paralogs in Schizosaccharomyces pombe (S. pombe). These two proteins have 90% amino acid similarity and are highly ++ conserved in eukaryotes. However, loss of rpl2702 , but not rpl2701 , alleviates the + growth defects caused by loss of elf1 , an AAA+ ATPase Elf1 (Elongation-like-Factor 1) involved in genome stability. This suggests, despite their high degree of similarity, Rpl2702 and Rpl2701 ribosomes may regulate the translation of different mRNA transcripts. I investigated the functional divergence between Rpl2701 and Rpl2702 and found rpl2702+ produces more RNA, while rpl2701+ produces more protein. Also, loss of the rpl2701+ results in a more severe growth defect and disrupts ribosome formation and + translation more drastically than the loss of rpl2702 . Additionally, I generated a series of Rpl27 chimeric proteins that supports the specialized functions of the Rpl27 paralogs. Finally, I show asymmetric RNA expression patterns for various duplicated ribosome paralog genes in S. pombe under normal and various stress conditions. This study is pivotal as it explores the debated question of whether cells produce specialized ribosomes.

subject

Functional Heterogeneity

Ribosome

Ribosome Protein Paralogs

Ribosome Proteins

Rpl27

S. pombe

contributor

Reid, Ke (advisor)

Alexander, Rebecca (committee member)

Currie, Joshua (committee member)

date

2024-02-13T09:36:24Z (accessioned)

2023 (issued)

degree

Biology (discipline)

embargo

2026-02-12 (terms)

2026-02-12 (liftdate)

identifier

http://hdl.handle.net/10339/102919 (uri)

language

en (iso)

publisher

Wake Forest University

type

Thesis