Related Experiment Video
Updated: Dec 14, 2025
04:25
Enriching Subcellular Proteins in Leptospira Using a Triton X-114-Based Fractionation Approach
Published on: August 8, 2025
1.1K
The predicted subcellular localisation of the sugarcane proteome
Renato Vicentini1, Marcelo Menossi1
1Departamento de Genética e Evolução, Laboratório de Genoma Funcional, Instituto de Biologia, CP 6109, Universidade Estadual de Campinas - UNICAMP, 13083-970, Campinas, SP, Brazil.
Functional Plant Biology : FPB
|July 22, 2020
Summary
This study analyzed sugarcane protein locations within cells. Most proteins reside in the nucleus, cytosol, mitochondria, or secretory pathways, with some found in multiple locations.
Area of Science:
- Plant Cell Biology
- Proteomics
- Bioinformatics
Background:
- Subcellular localization is crucial for protein function in highly organized plant cells.
- Predicting protein localization aids in understanding proteins with unknown or putative functions.
Purpose of the Study:
- To conduct the first in silico genome-wide subcellular localization analysis of the sugarcane transcriptome.
- To identify potential dual-targeted sugarcane proteins.
Main Methods:
- In silico genome-wide analysis of 11,882 predicted sugarcane proteins.
- Computational prediction of subcellular localization.
Main Results:
- The majority of sugarcane proteins are localized in the nucleus (44%), cytosol (19%), mitochondria (12%), and secretory destinations (11%).
- Approximately 19% of proteins were predicted to be localized in multiple cellular compartments.
- Identified a potential set of sugarcane proteins exhibiting dual targeting.
Conclusions:
- This study provides foundational knowledge on the subcellular proteome of sugarcane.
- The findings offer insights into protein function and potential regulatory mechanisms in sugarcane cells.
Related Concept Videos
01:24Oligosaccharide Assembly
3.4K
Protein glycosylation starts in the ER lumen and continues in the Golgi apparatus. Glycosyltransferases catalyze the addition of sugar molecules or glycosylation of proteins. Usually, these enzymes add sugars to the hydroxyl groups of selected serine or threonine residues to form O-linked glycans or the amino groups of asparagine residues to form N-linked glycans. Different positions on the same polypeptide chain can contain differently linked glycans.
Multiple sugar molecules that may or may...
Multiple sugar molecules that may or may...
3.4K
01:27Post-translational Translocation of Proteins to the RER
7.2K
A sizable fraction of proteins destined for ER are first synthesized in the cell cytosol and then transported across the ER membrane–a process called post-translational translocation. Similar to cotranslationally translocated proteins, these proteins also use the Sec translocon complex to enter the ER lumen.
Targeting proteins to the ER
Hsp40 and Hsp70 chaperone molecules bind the translated proteins in the cytosol to prevent their folding. The chaperone binding helps to keep the signal...
Targeting proteins to the ER
Hsp40 and Hsp70 chaperone molecules bind the translated proteins in the cytosol to prevent their folding. The chaperone binding helps to keep the signal...
7.2K
01:49Golgi Apparatus
99.2K
As they leave the Endoplasmic Reticulum (ER), properly folded and assembled proteins are selectively packaged into vesicles. These vesicles are transported by microtubule-based motor proteins and fuse together to form vesicular tubular clusters, subsequently arriving at the Golgi apparatus, a eukaryotic endomembrane organelle that often has a distinctive ribbon-like appearance.
99.2K
01:18Protein Transport to the Inner Chloroplast Membrane
2.3K
Proteins targeted to the inner chloroplast membrane, or plastid proteins, are transported by two general pathways: the stop-transfer and the re-insertion or post-import pathways. Most plastid proteins carry N-terminal transit sequences and internal import sequences targeting it to the specific chloroplast subcompartment. Proteins targeted by the stop-transfer pathway have internal hydrophobic sequences that inhibit their translocation into the stroma. As a result, these precursors are arrested...
2.3K
01:24Protein Transport to the Stroma
2.1K
Chloroplasts are triple membrane structures with an outer membrane, an inner membrane, and a thylakoid membrane, each containing distinct metabolite transporters, membrane translocons, and enzymes. Appropriate sorting and translocating these proteins to their correct membrane systems is essential for chloroplast function.
Protein complexes called the translocon of the outer chloroplast membrane or TOC complex, and the translocon of the inner chloroplast membrane or TIC complex mediate the...
Protein complexes called the translocon of the outer chloroplast membrane or TOC complex, and the translocon of the inner chloroplast membrane or TIC complex mediate the...
2.1K
01:11Protein Transport to the Outer Chloroplast Membrane
2.2K
Chloroplast outer membrane proteins encoded by the nucleus are synthesized in the cytosol. Soon after synthesis, they bind cytosolic factors such as 14-3-3 protein and the Hsp70 chaperones that keep these precursors in an unfolded state until their translocation.
Two models describe the mechanism of precursor recognition and entry across the outer membrane through the TOC complex. Model 1 suggests the newly synthesized precursor binds to the TOC receptor 159 and forms a complex.
Two models describe the mechanism of precursor recognition and entry across the outer membrane through the TOC complex. Model 1 suggests the newly synthesized precursor binds to the TOC receptor 159 and forms a complex.
2.2K