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Related Concept Videos

Histone Modification02:32

Histone Modification

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.
Acetylation
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Spreading of Chromatin Modifications

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.
Writers
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Chromatin Structure Regulates pre-mRNA Processing

In eukaryotic cells, nascent mRNA transcripts need to undergo many post-transcriptional modifications to reach the cell cytoplasm and translate into functional proteins. For a long time, transcription and pre-mRNA processing were considered two independent events that occur sequentially in the cell. However, it has now been well established that transcription and pre-mRNA processing are two simultaneous processes that are precisely regulated inside the cell.
The chromatin structure, especially...
Structure of a Gene01:30

Structure of a Gene

A gene is the fundamental unit of heredity. Every individual has two copies of each gene, one inherited from each parent. Although most people contain the same genes, there is a small fraction that is slightly different amongst people. A gene with a small difference in its sequence of DNA bases forms different alleles, contributing to different phenotypes.
However, only 1% of the DNA is composed of genes that encode proteins; the rest, 99% is non-coding DNA. This non-coding DNA performs...
Histone Modification02:32

Histone Modification

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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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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Preparation of Hydroxy-PAAm Hydrogels for Decoupling the Effects of Mechanotransduction Cues
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Genetically Modifying the Protein Matrix of Macroscopic Living Materials to Control Their Structure and Rheological

Esther M Jimenez1, Carlson Nguyen1, Ahmad Shakeel2

  • 1Department of BioSciences, Rice University, Houston, Texas 77005, United States.

ACS Synthetic Biology
|November 27, 2024
PubMed
Summary

Engineering living materials (ELMs) can be tuned by altering protein sequences. This study reveals how changing elastin-like polypeptide (ELP) length in Caulobacter crescentus ELMs impacts their structure and rheological properties.

Keywords:
elastin-like polypeptide (ELP)engineered living materialsmicrostructureprotein matrixrheological properties

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Area of Science:

  • Biomaterials Engineering
  • Synthetic Biology
  • Rheology

Background:

  • Engineering living materials (ELMs) aims to create cell-based materials with tunable properties.
  • Understanding sequence-structure-property relationships in ELMs is crucial but remains largely unexplored.
  • Synthetic biology has enabled modification of ELM rheology, but underlying mechanisms require further investigation.

Purpose of the Study:

  • To investigate how varying elastin-like polypeptide (ELP) length affects the microstructure and viscoelastic behavior of Caulobacter crescentus-based ELMs.
  • To elucidate the sequence-structure-property paradigm in engineered living materials.
  • To identify new design principles for tailoring ELM rheological properties through genetic modification.

Main Methods:

  • Engineered centimeter-scale ELMs using Caulobacter crescentus with varying ELP lengths.
  • Analyzed the impact of ELP length on material microstructure using microscopy techniques.
  • Characterized the viscoelastic behavior of ELMs under different conditions, including flow, to determine rheological properties.

Main Results:

  • Shortened ELP length resulted in thicker fibers and a stiffer material at rest.
  • Midlength ELP formed complex structures with increased yield stress under flow.
  • Lengthened ELP produced thinner strands with rheological properties similar to the midlength variant.

Conclusions:

  • Genetic sequence modifications, specifically ELP length, significantly alter ELM microstructure and rheological properties.
  • The study reveals complex sequence-structure-property relationships in ELMs, distinct from other biocomposite models.
  • Fine-tuning genetic sequences offers a powerful strategy for designing and controlling ELM behavior.