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Covalently Linked Protein Regulators

Covalently Linked Protein Regulators

Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
These groups modify specific amino acids in a protein.

Translocation of Proteins into the Mitochondria

Translocation of Proteins into the Mitochondria

Mitochondrial precursors are translocated to the internal subcompartments via independent mechanisms involving distinct protein machineries called translocases.
Sorting of outer membrane proteins:
Mitochondrial outer membrane proteins are of two types: the transmembrane, beta-barrel porins, and the membrane-anchored, alpha-helical proteins. Beta-barrel porin precursors are translocated by the TOM complex and inserted into the outer mitochondrial membrane by the SAM complex. In contrast,...

Post-translational Translocation of Proteins to the RER

Post-translational Translocation of Proteins to the RER

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...

Protein Modifications in the RER

Protein Modifications in the RER

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.
Broadly, these modifications can be categorized into four main categories — glycosylation, formation of disulfide bonds, assembly of protein subunits, and specific proteolytic cleavages like removal of signal sequences.

Microtubule Associated Proteins (MAPs)

Microtubule Associated Proteins (MAPs)

Microtubule function and architecture are regulated by an array of specialized proteins called microtubule-associated proteins or MAPs. These proteins are widespread across different organisms and have conserved protein motifs, like the multi-TOG domain for tubulin binding found in the CLASP family of MAPs. Some MAPs are lineage-specific based on their conserved domains. Their functions depend upon the cytoskeletal architecture and cell type they are located within. In-plant cells, a specific...

Bacterial Protein Maturation

Bacterial Protein Maturation

Bacterial protein maturation is a tightly regulated process that ensures newly synthesized polypeptides achieve correct functional conformations. This maturation involves a series of modifications, folding events, and quality control steps, often assisted by specialized chaperone proteins.N-Terminal ModificationsThe maturation of bacterial polypeptides begins cotranslationally as the polypeptide exits the ribosome. The first amino acid, N-formylmethionine (fMet), is typically modified at the...

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Related Experiment Video

Updated: Jul 4, 2026

Isolation of Intermediate Filament Proteins from Multiple Mouse Tissues to Study Aging-associated Post-translational Modifications

Isolation of Intermediate Filament Proteins from Multiple Mouse Tissues to Study Aging-associated Post-translational Modifications

Published on: May 18, 2017

High mobility group proteins and their post-translational modifications.

Qingchun Zhang¹, Yinsheng Wang

¹Department of Chemistry, University of California, Riverside, CA 92521-0403, USA.

Biochimica Et Biophysica Acta

|June 3, 2008

Summary

High mobility group (HMG) proteins regulate DNA processing via interactions modulated by post-translational modifications (PTMs). This review details HMG protein PTMs and their impact on cellular functions.

More Related Videos

Utilizing a Comprehensive Immunoprecipitation Enrichment System to Identify an Endogenous Post-translational Modification Profile for Target Proteins

Published on: January 8, 2018

Related Experiment Videos

Last Updated: Jul 4, 2026

Isolation of Intermediate Filament Proteins from Multiple Mouse Tissues to Study Aging-associated Post-translational Modifications

Isolation of Intermediate Filament Proteins from Multiple Mouse Tissues to Study Aging-associated Post-translational Modifications

Published on: May 18, 2017

Utilizing a Comprehensive Immunoprecipitation Enrichment System to Identify an Endogenous Post-translational Modification Profile for Target Proteins

Published on: January 8, 2018

Area of Science:

Molecular Biology
Chromatin Biology
Epigenetics

Background:

High mobility group (HMG) proteins are nuclear proteins crucial for DNA processing and chromatin organization.
HMG proteins (HMGA, HMGB, HMGN) dynamically interact with DNA, nucleosomes, and protein complexes.
Like histones, HMG proteins undergo extensive post-translational modifications (PTMs).

Purpose of the Study:

To review identified covalent modifications of HMG proteins.
To highlight the functional impact of HMG protein PTMs on cellular processes.
To underscore the complex interplay between HMG PTMs and their biological activities.

Main Methods:

Literature review of identified covalent modifications in HMG proteins.
Analysis of studies detailing the functional consequences of HMG protein PTMs.
Synthesis of information on how PTMs modulate HMG protein interactions.

Main Results:

Various PTMs, including acetylation, methylation, and phosphorylation, are identified on HMG proteins.
These modifications reversibly alter HMG protein interactions with DNA and other proteins.
PTMs significantly influence the diverse biological roles of HMG proteins.

Conclusions:

Post-translational modifications are critical regulators of HMG protein function.
Understanding HMG protein PTMs provides insight into DNA processing and chromatin regulation.
Further research into HMG PTMs will illuminate their roles in various cellular contexts.