A5004360679- Nuclear Structure and Function
- RNA Research and Splicing
- Genomics and Chromatin Dynamics
- Biotin and Related Studies
- Ubiquitin and proteasome pathways
- Fungal and yeast genetics research
- Enzyme Structure and Function
- RNA and protein synthesis mechanisms
- RNA modifications and cancer
- Mitochondrial Function and Pathology
- S100 Proteins and Annexins
- Viral Infections and Immunology Research
- Protein Structure and Dynamics
- Plant Surface Properties and Treatments
- Signaling Pathways in Disease
- DNA Repair Mechanisms
- Liver Disease Diagnosis and Treatment
- Drug Transport and Resistance Mechanisms
- Microbial Metabolic Engineering and Bioproduction
- melanin and skin pigmentation
- Microtubule and mitosis dynamics
- thermodynamics and calorimetric analyses
- Heat shock proteins research
- Hepatitis B Virus Studies
- DNA and Nucleic Acid Chemistry
The University of Texas Southwestern Medical Center
2020-2025
Universidade Estadual Paulista (Unesp)
2014-2020
University of British Columbia
2017
We explored how the number of structures is determined in an intracellular organelle series. In Tetrahymena, oral apparatus contains three diagonal ciliary rows: M1, M2, and M3. During development, M rows emerge by sequential segmentation a group basal bodies, starting with longest most anterior M1 ending shortest posterior The mpD-1 mpH-1 alleles increase decrease rows, respectively. identify MpH as TPR protein MpD importin-9. Both proteins localize to form concentration gradients. row...
IMPORTIN-4, the primary nuclear import receptor of core histones H3 and H4, binds H3–H4 dimer histone chaperone ASF1 prior to import. However, how H3–H3–ASF1 is recognized for transport cannot be explained by available crystal structures IMPORTIN-4–histone tail peptide complexes. Our 3.5-Å IMPORTIN-4–H3–H4–ASF1 cryoelectron microscopy structure reveals full complex shows a binding mode different from suggested previous structures. The N-terminal half IMPORTIN-4 clamps globular domain αN...
Neurospora crassa is a filamentous fungus that has been extensively studied as model organism for eukaryotic biology, providing fundamental insights into cellular processes such cell signaling, growth and differentiation. To advance in the study of this multicellular organism, an understanding specific mechanisms protein transport nucleus essential. Importin-α (Imp-α) receptor cargo proteins contain nuclear localization signals (NLSs) play key role classical import pathway. Structures Imp-α...
Environmental pH induces a stress response triggering signaling pathway whose components have been identified and characterized in several fungi. Neurospora crassa shares all six of the Aspergillus nidulans pathway, we investigate here their regulation during an alkaline response. We show that N. pal mutant strains, with exception Δpal-9, which is A. palI homolog, exhibit low conidiation are unable to grow at pH. Moreover, they accumulate pigment melanin, most likely via tyrosinase gene by...
Neurospora crassa has been widely used as a model organism and contributed to the development of biochemistry molecular biology by allowing identification many metabolic pathways mechanisms responsible for gene regulation. Nuclear proteins are synthesized in cytoplasm need be translocated nucleus exert their functions which importin-α receptor key role classical nuclear import pathway. In an attempt get structural information transport process N. crassa, we present herein cloning,...
The Neurospora crassa NIT-2 transcription factor belongs to the GATA family and plays a fundamental role in regulation of nitrogen metabolism. Because acts by accessing DNA inside nucleus, understanding nuclear import process is necessary characterize its function. Thus, present study, transport was investigated using combination biochemical, cellular, biophysical methods. A complemented strain that produced an sfGFP-NIT-2 fusion protein constructed, localization assessments were made under...
Abstract Importin-α (Impα) is an adaptor protein that binds to cargo proteins (containing Nuclear Localization Sequences - NLSs), for their translocation the nucleus. The specificities of Impα/NLS interactions have been studied, since these features could be used as important tools find potential NLSs in nuclear or even development targets inhibit import design peptides drug delivery. Few structural studies compared different Impα variants from same organism organisms. Previously, we...
Core histones, synthesized and processed in the cytoplasm, must be chaperoned as they are transported into nucleus for nucleosome assembly. The importin Kap114 transports H2A-H2B yeast nucleus, where RanGTP facilitates histone release. also bind chaperone Nap1, but how Nap1 cooperate transport assembly remains unclear. Here, biochemical structural analyses show that Kap114, H2A-H2B, a dimer (Nap12) associate absence presence of to form equimolar complexes. A previous study had shown reduces...
Importin-α recognizes cargo proteins that contain classical nuclear localization sequences (NLS) and, in complex with importin-β, is able to translocate through the pore complex. The filamentous fungus Neurospora crassa a well studied organism has been widely used as model for fundamental aspects of eukaryotic biology, and important understanding specific mechanisms protein transport cell nucleus. In this work, crystallization preliminary X-ray diffraction analysis importin-α from N....
Abstract Importin-4 is the primary nuclear import receptor of core histones H3 and H4. binds H3-H4 dimer histone-chaperone ASF1 prior to import, but available structures Importin-4·histone tail complexes do not explain how recognizes biologically relevant heterotrimeric H3-H4·ASF1 cargo. Our 3.5 Å Importin-4·H3-H4·ASF1 cryo-electron microscopy structure revealed interactions with different those suggested by previous Importin-H3 peptide structures. The N-terminal half clamps globular histone...
Core histones are synthesized and processed in the cytoplasm before transport into nucleus for assembly nucleosomes; however, they must also be chaperoned as free toxic. The importin Kap114 binds transports histone H2A-H2B yeast nucleus, where RanGTP facilitates release. bind Nap1 chaperone, which is found both but how cooperate processing nucleosome has been unclear. To understand these mechanisms, we used biochemical structural analyses to reveal Nap1, Kap114, interact. We show that a dimer (Nap1
Neurospora crassa has been widely used as a model organism and contributed to the development of biochemistry molecular biology by allowing identification many metabolic pathways mechanisms responsible for gene regulation. Nuclear proteins are synthesized in cytoplasm need be translocated nucleus exert their functions which importin-α receptor key role classical nuclear import pathway. In an attempt get structural information transport process N. crassa, we present herein cloning,...
Importin‐α (Impα) is a protein that mediates nuclear import of macromolecules via recognition localization sequences in the macromolecule will be transported. Some proteins and transcription factors related with nitrogen glycogen metabolism fungus possess putative NLSs, suggesting they can transported into nucleus classical pathway, which mediated by Impα Importin‐β. This work presents biophysical functional experiments confirms interaction between from Neurospora crassa (NcImpα) Mus...