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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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Updated: Sep 15, 2025

Xenopus laevis as a Model to Identify Translation Impairment

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Decoding mEos4b day-long maturation and engineering fast-maturing variants.

Arijit Maity¹, Oleksandr Glushonkov², Isabel Ayala¹

¹Univ. Grenoble Alpes, CEA, CNRS, Institut de Biologie Structurale, Grenoble, France.

Protein Science : a Publication of the Protein Society

|July 17, 2025

Summary

This summary is machine-generated.

Researchers improved the maturation speed of fluorescent proteins, crucial for microscopy. They engineered mEos4b variants to mature much faster, enhancing cellular imaging without losing brightness.

Keywords:

NMR X‐ray crystallography chromophore fluorescent proteins maturation protein engineering spectroscopy super resolution microscopy

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Area of Science:

Biophysics
Molecular Biology
Microscopy

Background:

Maturation speed of fluorescent proteins impacts cellular brightness, labeling efficiency, and temporal resolution in fluorescence microscopy.
Green-to-red photoconvertible fluorescent proteins (PCFPs) are vital for techniques like Photoactivated Localization Microscopy (PALM) and single-particle tracking, but slow maturation can limit their utility.

Purpose of the Study:

To systematically characterize the maturation speed of mEos-derived PCFPs.
To identify and engineer variants with accelerated maturation times for improved performance in advanced microscopy techniques.

Main Methods:

Systematic characterization of mEos-derived PCFP maturation in Escherichia coli.
Structure-guided mutagenesis strategy to modify PCFP properties.
Assessment of molecular brightness and photophysical performance under single-molecule imaging conditions.

Main Results:

Several mEos variants (mEos2, mEos3.1, mEos3.2, mEos4b) exhibit extremely slow maturation.
The oxidation step in these PCFPs was found to be rapid and not the rate-limiting factor in maturation.
Engineered mEos4b variants demonstrated a reduction in maturation time by nearly two orders of magnitude.

Conclusions:

Slow maturation of certain mEos-derived PCFPs can be a significant limitation for advanced microscopy.
Structure-guided mutagenesis is an effective strategy for accelerating PCFP maturation.
The developed mEos4b variants offer significantly faster maturation without compromising essential photophysical properties for single-molecule imaging.