Proteomic Identification of Small-Subunit Ribosome Assembly Factors in <i>Trypanosoma brucei</i>

. We generated cell lines expressing tagged versions of UTP6 and PNO1, two conserved ribosome biogenesis factors that provide complementary access to complexes of early SSU processome intermediates and later pre-40S maturation stages. Affinity purification followed by mass spectrometry identified numerous conserved ribosome biogenesis factors alongside a substantial set of trypanosomatid-specific proteins with no assigned function. Structural analyses revealed that many of these uncharacterized proteins contain predicted RNA-binding motifs or protein-protein interaction domains, and have been previously localized to the nucleolus, supporting potential roles in ribosome synthesis. Our findings expand the repertoire of candidate SSU assembly factors in kinetoplastids and highlight species-specific adaptations in ribosome biogenesis, providing a foundation for future functional studies targeting these unique components.

Authors

Institutions

Publication Details

Journal
Journal of Proteome Research
Published
2026-05-18
DOI
https://doi.org/10.1021/acs.jproteome.6c00066
Primary Topic
Trypanosoma species research and implications
Type
article
Field-Weighted Citation Impact
0.00

Funders

Controls
|||
ALL TIME
JAN
FEB
MAR
APR
MAY
JUN
JUL
AUG
SEP
OCT
article

Proteomic Identification of Small-Subunit Ribosome Assembly Factors in Trypanosoma brucei

B.G. Guimarães, Nilson Ivo Tonin Zanchin, Priscila Mazzocchi Hiraiwa, Gustavo Guadagnini Perez et al.
Journal of Proteome Research
Trypanosoma species research and implications
article

Proteomic Identification of Small-Subunit Ribosome Assembly Factors in Trypanosoma brucei

B.G. Guimarães, Nilson Ivo Tonin Zanchin, Priscila Mazzocchi Hiraiwa, Gustavo Guadagnini Perez, Verônica Santana da Silva
article en

Abstract

. We generated cell lines expressing tagged versions of UTP6 and PNO1, two conserved ribosome biogenesis factors that provide complementary access to complexes of early SSU processome intermediates and later pre-40S maturation stages. Affinity purification followed by mass spectrometry identified numerous conserved ribosome biogenesis factors alongside a substantial set of trypanosomatid-specific proteins with no assigned function. Structural analyses revealed that many of these uncharacterized proteins contain predicted RNA-binding motifs or protein-protein interaction domains, and have been previously localized to the nucleolus, supporting potential roles in ribosome synthesis. Our findings expand the repertoire of candidate SSU assembly factors in kinetoplastids and highlight species-specific adaptations in ribosome biogenesis, providing a foundation for future functional studies targeting these unique components.

Journal of Proteome Research
Naval Postgraduate School (US), Institute for Postgraduate Medical Education (CZ), Postgraduate Center for Mental Health (US), Tashkent Institute Of Postgraduate Medical Education (UZ), Fundação Carlos Chagas (BR), Universidade Federal do Paraná (BR)
Coordenação de Aperfeiçoamento de Pessoal de Nível Superior, Conselho Nacional de Desenvolvimento Científico e Tecnológico
Zero hunger
Openalex Percentile: Top 6%
Trypanosoma species research and implications
AI Navigator

Ask Laika to Summarize, Analyze, and Connect papers live on the map.

Summarize Papers & Methodologies

Extract key findings, datasets, and comparative methods across publications.

Benchmark Rankings & Visual Analytics

Rank top research institutions, authors, funders, topics, and journals by Field-Weighted Citation Impact (FWCI) and paper volume with instant charts.

Connect Distant Disciplines

Bridge topological clusters on the map to find hidden collaborative intersections.