Katrin Karbstein

ORCID: 0000-0002-4034-1331
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About
Contact & Profiles
Research Areas
  • RNA modifications and cancer
  • RNA and protein synthesis mechanisms
  • RNA Research and Splicing
  • Peptidase Inhibition and Analysis
  • Bacteriophages and microbial interactions
  • CRISPR and Genetic Engineering
  • Mechanisms of cancer metastasis
  • Autophagy in Disease and Therapy
  • Genomics and Phylogenetic Studies
  • Natural Compound Pharmacology Studies
  • Viral Infections and Immunology Research
  • Endoplasmic Reticulum Stress and Disease
  • Advanced biosensing and bioanalysis techniques
  • Mitochondrial Function and Pathology
  • Food and Agricultural Sciences
  • Fungal and yeast genetics research
  • Diverse Scientific Research Studies
  • X-ray Spectroscopy and Fluorescence Analysis
  • Toxoplasma gondii Research Studies
  • Radio, Podcasts, and Digital Media
  • Parasitic Infections and Diagnostics
  • Medicinal plant effects and applications
  • Protist diversity and phylogeny
  • Interdisciplinary Research and Collaboration
  • scientometrics and bibliometrics research

Vanderbilt University
2024-2025

Scripps Research Institute
2015-2024

The Herbert Wertheim UF Scripps Institute for Biomedical Innovation & Technology
2022-2024

Scripps (United States)
2021-2024

Towson University
2024

Howard Hughes Medical Institute
2018-2023

University of Florida
2022-2023

University of Montana
2021-2022

Scripps Institution of Oceanography
2021

University of Pennsylvania
2019

Ribosome assembly in eukaryotes requires approximately 200 essential factors (AFs) and occurs through ordered events that initiate the nucleolus culminate cytoplasm. Here, we present electron cryo-microscopy (cryo-EM) structure of a late cytoplasmic 40S ribosome intermediate from Saccharomyces cerevisiae at 18 angstrom resolution. We obtained cryo-EM reconstructions preribosomal complexes lacking individual components to define positions all seven AFs bound this intermediate. These...

10.1126/science.1208245 article EN Science 2011-08-12

Ribosome assembly is a hierarchical process that involves pre-rRNA folding, modification, and cleavage of ribosomal proteins. In eukaryotes, this requires macromolecular complex comprising over 200 proteins RNAs. Whereas the rRNA modification machinery well-characterized, to release mature rRNAs poorly understood, in yeast, only 2 8 endonucleases have been identified. The essential conserved ribosome factor Nob1 has suggested be endonuclease responsible for generating 3'-end 18S by cleaving...

10.1073/pnas.0905403106 article EN Proceedings of the National Academy of Sciences 2009-08-15

Although ribosome assembly is quality controlled to maintain protein homeostasis, different populations have been described. How these form, especially under stress conditions that affect energy levels and stop the energy-intensive production of ribosomes, remains unknown. Here, we demonstrate how a physiologically relevant population arises during high Na + , sorbitol, or pH via dissociation Rps26 from fully assembled ribosomes enable translational response stresses. The chaperone Tsr2...

10.1126/sciadv.abl4386 article EN cc-by-nc Science Advances 2022-02-25

The 18S rRNA sequence is highly conserved, particularly at its 3'-end, which formed by the endonuclease Nob1. How Nob1 identifies target not known, and in vitro experiments have shown to be error-prone. Moreover, around 3'-end degenerate with similar sites nearby. Here, we used yeast genetics, biochemistry, next-generation sequencing investigate a role for ATPase Rio1 monitoring accuracy of 3'-end. We demonstrate that can miscleave substrate miscleaved accumulates upon bypassing...

10.1371/journal.pbio.3001767 article EN cc-by PLoS Biology 2024-04-25

10.1038/s41556-024-01594-6 article EN Nature Cell Biology 2025-02-11

The hammerhead ribozyme crystal structure identified a specific metal ion binding site referred to as the P9/G10.1 site. Although this is ∼20 Å away from cleavage site, its disruption highly deleterious for catalysis. Additional published results have suggested that pro-RP oxygen at coordinated by in reaction's transition state. Herein, we report study on Cd2+ rescue of phosphorothioate substitution Under all conditions, concentration dependence can be accounted single rescuing ion. affinity...

10.1021/bi9913202 article EN Biochemistry 1999-10-01

Casein kinase 1δ/ε (CK1δ/ε) and their yeast homologue Hrr25 are essential for cell growth. Further, CK1δ is overexpressed in several malignancies, inhibitors have shown promise preclinical animal studies. However, the substrates of CK1δ/ε that necessary growth survival unknown. We show ribosome assembly, where it phosphorylates assembly factor Ltv1, which causes its release from nascent 40S subunits allows subunit maturation. inactivation or expression a nonphosphorylatable Ltv1 variant...

10.1083/jcb.201409056 article EN cc-by-nc-sa The Journal of Cell Biology 2015-03-16

In all forms of life, rRNAs for the small and large ribosomal subunit are co-transcribed as a single transcript. Although this ensures equimolar production rRNAs, it requires endonucleolytic separation pre-rRNAs to initiate rRNA production. yeast, processing primary transcript encoding 18 S, 5.8 25 S has been studied extensively. Nevertheless, most nucleases remain be identified. Here, we show that Rcl1, conserved in eukaryotes, cleaves pre-rRNA at so-called site A2, co-transcriptional...

10.1074/jbc.m111.268649 article EN cc-by Journal of Biological Chemistry 2011-08-18

The correct assembly of ribosomes from ribosomal RNAs (rRNAs) and proteins (RPs) is critical, as indicated by the diseases caused RP haploinsufficiency loss stoichiometry in cancer cells. Nevertheless, how each ensured remains poorly understood. We use yeast genetics, biochemistry, structure probing to show that factor Ltv1 facilitates incorporation Rps3, Rps10, Asc1/RACK1 into small subunit head. Ribosomes Ltv1-deficient have substoichiometric amounts Rps10 Asc1 defects translational...

10.1083/jcb.201804163 article EN cc-by-nc-sa The Journal of Cell Biology 2018-10-22

10.1016/j.jmb.2010.09.064 article EN Journal of Molecular Biology 2010-10-09
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