Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

Riboswitches01:56

Riboswitches

9.9K
Riboswitches are non-coding mRNA domains that regulate the transcription and translation of downstream genes without the help of proteins. Riboswitches bind directly to a metabolite and can form unique stem-loop or hairpin structures in response to the amount of the metabolite present. They have two distinct regions – a metabolite-binding aptamer and an expression platform.
The aptamer has high specificity for a particular metabolite which allows riboswitches to specifically regulate...
9.9K
Leaky Scanning02:28

Leaky Scanning

5.8K
During most eukaryotic translation processes, the small 40S ribosome subunit scans an mRNA from its 5' end until it encounters the first start AUG codon. The large 60S ribosomal subunit then joins the smaller one to initiate protein synthesis. The location of the translation initiation is largely determined by the nucleotides near the start codon as there may be multiple translation initiation sites present on the mRNA.  Marilyn Kozak discovered that the sequence RCCAUGG (where R...
5.8K
Peptidoglycan Synthesis01:28

Peptidoglycan Synthesis

3.4K
Structure of PeptidoglycanPeptidoglycan is a vital structural component of the bacterial cell wall, providing mechanical strength and shape to the cell. It consists of repeating units of two sugars—N-acetylglucosamine (NAG) and N-acetylmuramic acid (NAM)—linked by β-1,4 glycosidic bonds. These sugar chains are cross-linked by short peptide chains, forming a mesh-like polymer that surrounds the bacterial plasma membrane.Cytoplasmic Phase – Precursor SynthesisPeptidoglycan...
3.4K
Initiation of Translation02:33

Initiation of Translation

39.7K
Initiating translation is complex because it involves multiple molecules. Initiator tRNA, ribosomal subunits, and eukaryotic initiation factors (eIFs) are all required to assemble on the initiation codon of mRNA. This process consists of several steps that are mediated by different eIFs.
First, the initiator tRNA must be selected from the pool of elongator tRNAs by eukaryotic initiation factor 2 (eIF2). The initiator tRNA (Met-tRNAi) has conserved sequence elements including modified bases at...
39.7K
Amino Acid Biosynthetic Pathways01:29

Amino Acid Biosynthetic Pathways

1.5K
Amino acid biosynthesis is essential for cell growth, protein synthesis, and metabolic regulation. Cells generate essential and non-essential amino acids from metabolic intermediates to sustain vital biological functions. These intermediates originate from key metabolic pathways: glycolysis, the tricarboxylic acid (TCA) cycle, and the pentose phosphate pathway. Important precursors include α-ketoglutarate, pyruvate, oxaloacetate, phosphoenolpyruvate, and erythrose-4-phosphate, which...
1.5K
Translation in Prokaryotes01:29

Translation in Prokaryotes

2.0K
Prokaryote translation is a complex, highly coordinated process that converts genetic information from mRNA into functional proteins. It involves three stages: initiation, elongation, and termination, each facilitated by specific molecular components.Initiation of TranslationThe process begins with the assembly of the ribosomal subunits and initiation factors on the mRNA. In bacteria, the 30S ribosomal subunit recognizes the Shine-Dalgarno sequence in the mRNA, a conserved region upstream of...
2.0K

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

The inhibition of pathological IgE in allergic diseases by natural compounds.

Natural products and bioprospecting·2026
Same author

Intraoperative NIR-II fluorescence guidance for precise tumor margin assessment and maximized tissue preservation in breast surgery.

Breast cancer research : BCR·2026
Same author

Gut microbiota-dependent metabolism of 6-shogaol generates bioactive metabolites that mediate its anti-inflammatory effects.

Food & function·2026
Same author

Pathogen-Associated Molecular Pattern (PAMP)-Induced Peptide LcPIP1 Derived from Litchi Promotes the Resistance of Litchi Fruit against Litchi Downy Blight Caused by <i>Peronophythora litchii</i>.

Journal of agricultural and food chemistry·2026
Same author

Crosstalk between iron metabolism dysregulation and the oral microbiome in periodontitis.

Journal of oral microbiology·2026
Same author

PEYOLO: a wrist fracture detection network based on multi-level receptive field feature extraction and cross-scale fusion.

Frontiers in medicine·2026

Related Experiment Video

Updated: Mar 2, 2026

Antimicrobial Peptides Produced by Selective Pressure Incorporation of Non-canonical Amino Acids
11:56

Antimicrobial Peptides Produced by Selective Pressure Incorporation of Non-canonical Amino Acids

Published on: May 4, 2018

13.1K

Decoding and reprogramming fungal iterative nonribosomal peptide synthetases.

Dayu Yu1,2, Fuchao Xu2, Shuwei Zhang2

  • 1Department of Applied Chemistry and Biological Engineering, College of Chemical Engineering, Northeast Electric Power University, Jilin, Jilin 132012, China.

Nature Communications
|May 24, 2017
PubMed
Summary

Fungal iterative nonribosomal peptide synthetases (NRPSs) use a unique alternating precursor incorporation strategy to synthesize natural products. This study reveals their mechanism and offers a method for engineering NRPSs to create novel peptides.

More Related Videos

Residue-Specific Exchange of Proline by Proline Analogs in Fluorescent Proteins: How "Molecular Surgery" of the Backbone Affects Folding and Stability
10:31

Residue-Specific Exchange of Proline by Proline Analogs in Fluorescent Proteins: How "Molecular Surgery" of the Backbone Affects Folding and Stability

Published on: February 3, 2022

3.5K
Engineering 'Golden' Fluorescence by Selective Pressure Incorporation of Non-canonical Amino Acids and Protein Analysis by Mass Spectrometry and Fluorescence
11:51

Engineering 'Golden' Fluorescence by Selective Pressure Incorporation of Non-canonical Amino Acids and Protein Analysis by Mass Spectrometry and Fluorescence

Published on: April 27, 2018

12.5K

Related Experiment Videos

Last Updated: Mar 2, 2026

Antimicrobial Peptides Produced by Selective Pressure Incorporation of Non-canonical Amino Acids
11:56

Antimicrobial Peptides Produced by Selective Pressure Incorporation of Non-canonical Amino Acids

Published on: May 4, 2018

13.1K
Residue-Specific Exchange of Proline by Proline Analogs in Fluorescent Proteins: How "Molecular Surgery" of the Backbone Affects Folding and Stability
10:31

Residue-Specific Exchange of Proline by Proline Analogs in Fluorescent Proteins: How "Molecular Surgery" of the Backbone Affects Folding and Stability

Published on: February 3, 2022

3.5K
Engineering 'Golden' Fluorescence by Selective Pressure Incorporation of Non-canonical Amino Acids and Protein Analysis by Mass Spectrometry and Fluorescence
11:51

Engineering 'Golden' Fluorescence by Selective Pressure Incorporation of Non-canonical Amino Acids and Protein Analysis by Mass Spectrometry and Fluorescence

Published on: April 27, 2018

12.5K

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Natural Product Synthesis

Background:

  • Nonribosomal peptide synthetases (NRPSs) are crucial for producing diverse natural products.
  • The iterative catalytic mechanisms of bacterial NRPSs are well-understood, but fungal NRPS mechanisms remain largely unknown.
  • Understanding fungal NRPSs is key to unlocking novel peptide synthesis.

Purpose of the Study:

  • To elucidate the iterative catalytic mechanism of fungal NRPSs.
  • To investigate how fungal NRPSs control product length.
  • To develop a method for reprogramming fungal NRPSs for novel peptide synthesis.

Main Methods:

  • Analysis of beauvericin and bassianolide synthetase domain organization (C1-A1-T1-C2-A2-MT-T2a-T2b-C3).
  • In vitro reconstruction of beauvericin biosynthesis using specific enzyme domains and SNAC-linked precursors.
  • Domain swapping experiments to alter NRPS product length.

Main Results:

  • Fungal iterative NRPSs employ an alternating precursor incorporation strategy.
  • The C3 and C2 domains sequentially incorporate precursors, with the growing chain interacting with T1 and T2a/T2b domains.
  • The C3 domain cyclizes the depsipeptide chain upon reaching the full length.
  • Successful in vitro reconstruction of beauvericin biosynthesis was achieved.
  • A domain swapping approach demonstrated the ability to reprogram NRPS length.

Conclusions:

  • Fungal NRPS mechanisms differ significantly from bacterial NRPSs, particularly in iterative synthesis and product length control.
  • The findings provide a mechanistic framework for fungal NRPSs.
  • This work enables the enzymatic synthesis of non-natural nonribosomal peptides with tailored lengths.