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Protein Modifications in the RER

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Modification of secretory and transmembrane proteins entering the rough ER begins in the ER lumen. These modifications aid in protein folding and stabilize the acquired tertiary structure. Protein modifications in the rough ER co-occur at different stages of protein folding.
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The histone proteins have a flexible N-terminal tail extending out from the nucleosome. These histone tails are often subjected to post-translational modifications such as acetylation, methylation, phosphorylation, and ubiquitination. Particular combinations of these modifications form “histone codes” that influence the chromatin folding and tissue-specific gene expression.
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Pre-mRNA Processing: Modification of pre-mRNA Ends

Pre-mRNA Processing: Modification of pre-mRNA Ends

In eukaryotic cells, transcripts made by RNA polymerase are modified and processed before exiting the nucleus. Unprocessed RNA is called precursor mRNA or pre-mRNA to distinguish it from mature mRNA.
Once about 20-40 ribonucleotides have been joined together by RNA polymerase, a group of enzymes adds a cap to the 5' end of the growing transcript. In this process, a 5' phosphate is replaced by modified guanosine that has a methyl group attached (7-methyl guanosine). This 5' cap helps...

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The histone proteins in the nucleosomes are post-translationally modified (PTM) to increase or decrease access to DNA. The commonly observed PTMs are methylation, acetylation, phosphorylation, and ubiquitination of lysine amino acids in the histone H3 tail region. These histone modifications have specific meaning for the cell. Hence, they are called "histone code". The protein complex involved in histone modification is termed as "reader-writer" complex.
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Related Experiment Video

Updated: Jan 28, 2026

Identification of Post-translational Modifications of Plant Protein Complexes

Identification of Post-translational Modifications of Plant Protein Complexes

Published on: February 22, 2014

Cocoa Bean Proteins-Characterization, Changes and Modifications due to Ripening and Post-Harvest Processing.

Harshadrai M Rawel¹, Gerd Huschek², Sorel Tchewonpi Sagu³

¹Institute of Nutritional Science, University of Potsdam, Arthur-Scheunert-Allee 114-116, 14558 Nuthetal, Potsdam, Germany. rawel@uni-potsdam.de.

|February 23, 2019

Summary

Cocoa protein fractions significantly impact bioactive potential and sensory traits. Processing stages like fermentation and roasting alter these proteins, offering opportunities for functional foods.

Keywords:

bioactive peptides classification cocoa processing cocoa proteins extraction and characterization methods fermentation-related enzymes heath potentials protein–phenol interactions

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Area of Science:

Food Science
Biochemistry
Agricultural Science

Background:

Cocoa protein fractions influence bioactive potential and sensory properties.
Understanding protein changes during cultivation and processing is crucial for cocoa product development.

Purpose of the Study:

To review the impact of cultivation and processing on cocoa protein fractions.
To focus on major seed storage proteins and their modifications.
To elucidate the bioactive potential derived from cocoa proteins.

Main Methods:

Review of extraction and characterization methods for cocoa proteins.
Analysis of protein classification approaches over time.
Documentation of protein composition changes during seed maturation and post-harvest processing (fermentation, drying, roasting).

Main Results:

Protein fractions undergo significant changes during cocoa seed development and post-harvest treatments.
Fermentation, drying, and roasting notably modify cocoa protein composition.
Cocoa proteins contribute to the overall bioactive potential of cocoa products.

Conclusions:

Further research into other bioactive cocoa components is needed, considering roasting-induced reaction products.
Partially processed cocoa beans (e.g., fermented) offer a rich source of bioactive proteins for functional food applications.