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RVB-1 and RVB-2 are stress responsive proteins in Neurospora crassa and RVB-1 interacts with the centromeric

Jonatas Erick Maimoni Campanella^1,2, Paula Aboud Barbugli³, Antoniel Augusto Severo Gomes⁴

¹Departamento de Bioquímica e Química Orgânica, Instituto de Química, Universidade Estadual Paulista, UNESP, Araraquara, SP, Brazil.

The FEBS Journal

|July 6, 2026

Summary

Neurospora crassa RVB proteins are crucial stress sensors, modulating gene expression and localization under stress. They interact with new partners, revealing roles in metabolism and centromere maintenance.

Keywords:

Neurospora crassa RVB‐1 RVB‐2 protein interaction shugoshin stress response

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Published on: January 8, 2015

Area of Science:

Molecular Biology
Cell Biology
Biochemistry

Background:

RVB-1 and RVB-2 proteins are AAA+ superfamily members in a complex essential for cellular processes.
While linked to cancer, their novel functions are under investigation.

Purpose of the Study:

To investigate the role of RVB-1 and RVB-2 in the stress response of Neurospora crassa.
To identify new molecular functions and interaction partners of RVB-1.

Main Methods:

Gene and protein expression analysis
Cellular localization studies
Immunoprecipitation followed by mass spectrometry
Genetic and biochemical interaction assays
AlphaFold3 structural analysis

Main Results:

RVB-1 and RVB-2 expression and localization are modulated by stress (temperature, salt, light).
These proteins form cytoplasmic granules induced by stress.
Identified new RVB-1 interactors involved in chromatin remodeling, metabolism, and cell signaling.
Discovered a novel interaction between RVB-1 and shugoshin (SGO-1), suggesting a role in centromere maintenance.

Conclusions:

RVB proteins function as stress sensors in N. crassa.
RVB-1 has a newly identified role in centromeric region maintenance through interaction with SGO-1.
The findings highlight the importance of RVBs in cellular metabolism and stress response.