Search research articles

ABOUT JoVE

Overview Leadership Blog JoVE Help Center

AUTHORS

Publishing Process Editorial Board Scope & Policies Peer Review FAQ Submit

LIBRARIANS

Testimonials Subscriptions Access Resources Library Advisory Board FAQ

RESEARCH

JoVE Journal Methods Collections JoVE Encyclopedia of Experiments Archive

EDUCATION

JoVE Core JoVE Business JoVE Science Education JoVE Lab Manual Faculty Resource Center Faculty Site

Terms & Conditions of Use

Related Concept Videos

The Calvin Benson Cycle

The Calvin Benson Cycle

Ribulose 1,5- bisphosphate carboxylase/oxygenase (RuBisCo) is a critical enzyme that catalyzes carbon dioxide assimilation during photosynthesis. However, it is an inefficient enzyme, having an extremely slow catalytic rate. A typical enzyme can process about a thousand molecules per second; however, RuBisCo fixes only around three-carbon dioxides per second. Photosynthetic cells compensate for this slow rate by synthesizing very high amounts of RuBisCo, making it the most abundant single...

The Supercomplexes in the Crista Membrane

The Supercomplexes in the Crista Membrane

The mitochondrial cristae membrane is the primary site for the oxidative phosphorylation (OXPHOS) process of energy conversion mediated through respiratory complexes I to V. These complexes have been widely studied for decades, and it has been proven that they form supramolecular structures called respiratory supercomplexes (SC). These higher-order complexes may be crucial in maintaining the biochemical structure and improving the physiological activity of the individual complexes while...

Ribosomes

Ribosomes

Ribosomes translate genetic information encoded by messenger RNA (mRNA) into proteins. Both prokaryotic and eukaryotic cells have ribosomes. Cells that synthesize large quantities of protein—such as secretory cells in the human pancreas—can contain millions of ribosomes.Ribosome Structure and AssemblyRibosomes are composed of ribosomal RNA (rRNA) and proteins. In eukaryotes, rRNA is transcribed from genes in the nucleolus—a part of the nucleus that specializes in ribosome production. Within the...

Ribosomes

Ribosomes

Ribosomes translate genetic information encoded by messenger RNA (mRNA) into proteins. Both prokaryotic and eukaryotic cells have ribosomes. Cells that synthesize large quantities of protein—such as secretory cells in the human pancreas—can contain millions of ribosomes.
Ribosome Structure and Assembly
Ribosomes are composed of ribosomal RNA (rRNA) and proteins. In eukaryotes, rRNA is transcribed from genes in the nucleolus—a part of the nucleus that specializes in ribosome production. Within...

Ribosomes

Ribosomes

Ribosomes translate genetic information encoded by messenger RNA (mRNA) into proteins. Both prokaryotic and eukaryotic cells have ribosomes. Cells that synthesize large quantities of protein—such as secretory cells in the human pancreas—can contain millions of ribosomes.
Ribosome Structure and Assembly
Ribosomes are composed of ribosomal RNA (rRNA) and proteins. In eukaryotes, rRNA is transcribed from genes in the nucleolus—a part of the nucleus that specializes in ribosome production. Within...

Ribosomes

Ribosomes

Ribosomes translate genetic information encoded by messenger RNA (mRNA) into proteins. Both prokaryotic and eukaryotic cells have ribosomes. Cells that synthesize large quantities of protein—such as secretory cells in the human pancreas—can contain millions of ribosomes.Ribosome Structure and AssemblyRibosomes are composed of ribosomal RNA (rRNA) and proteins. In eukaryotes, rRNA is transcribed from genes in the nucleolus—a part of the nucleus that specializes in ribosome production. Within the...

You might also read

Related Articles

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

Sort by

Same author

DiRT v2.0: An Optimized Pipeline for Detecting Dicistronic tRNA-mRNA Transcripts in Plants.

Bio-protocol·2026

Same author

MscM uses a novel gating mechanism for bacterial mechanosensitive channels.

bioRxiv : the preprint server for biology·2026

Same author

Ideal efficacy photoswitching for chromocontrol of TRPC4/5 channel functions in live tissues.

Nature chemical biology·2026

Same author

Carbon source-induced changes in the transcriptional landscape of Novacetimonas hansenii.

Bioresource technology·2026

Same author

The resting and ligand-bound states of the membrane-embedded human T-cell receptor-CD3 complex.

Nature communications·2025

Same author

Spatial N-glycan rearrangement on α<sub>5</sub>β<sub>1</sub> integrin nucleates galectin-3 oligomers to determine endocytic fate.

Nature communications·2025

Search research articles

Related Experiment Video

Updated: Jun 25, 2026

Methylated RNA Immunoprecipitation Assay to Study m5C Modification in Arabidopsis

Methylated RNA Immunoprecipitation Assay to Study m⁵C Modification in Arabidopsis

Published on: May 14, 2020

Rubisco in complex with Rubisco large subunit methyltransferase.

Stefan Raunser¹, Roberta Magnani, Zhong Huang

¹Department of Cell Biology and Howard Hughes Medical Institute, Harvard Medical School, Boston, MA 02115, USA. raunser@mpidortmund.mpg.de

Proceedings of the National Academy of Sciences of the United States of America

|February 12, 2009

Summary

This study reveals the structural basis of Rubisco methylation by Rubisco large subunit methyltransferase (RLSMT), a key enzyme in photosynthesis. The findings offer insights into enzyme-substrate interactions and potential catalytic mechanisms.

More Related Videos

Evaluation of Photosynthetic Efficiency in Photorespiratory Mutants by Chlorophyll Fluorescence Analysis

Evaluation of Photosynthetic Efficiency in Photorespiratory Mutants by Chlorophyll Fluorescence Analysis

Published on: December 9, 2022

Artificial RNA Polymerase II Elongation Complexes for Dissecting Co-transcriptional RNA Processing Events

Artificial RNA Polymerase II Elongation Complexes for Dissecting Co-transcriptional RNA Processing Events

Published on: May 13, 2019

Related Experiment Videos

Last Updated: Jun 25, 2026

Methylated RNA Immunoprecipitation Assay to Study m5C Modification in Arabidopsis

Methylated RNA Immunoprecipitation Assay to Study m⁵C Modification in Arabidopsis

Published on: May 14, 2020

Evaluation of Photosynthetic Efficiency in Photorespiratory Mutants by Chlorophyll Fluorescence Analysis

Evaluation of Photosynthetic Efficiency in Photorespiratory Mutants by Chlorophyll Fluorescence Analysis

Published on: December 9, 2022

Artificial RNA Polymerase II Elongation Complexes for Dissecting Co-transcriptional RNA Processing Events

Artificial RNA Polymerase II Elongation Complexes for Dissecting Co-transcriptional RNA Processing Events

Published on: May 13, 2019

Area of Science:

Biochemistry
Structural Biology
Enzymology

Background:

SET domain protein lysine methyltransferases (PKMTs) are crucial enzymes involved in epigenetic regulation and cancer.
Rubisco large subunit methyltransferase (RLSMT) methylates Rubisco, an essential photosynthetic enzyme, at lysine-14.

Purpose of the Study:

To elucidate the structural mechanism of Rubisco methylation by RLSMT.
To provide the first structural analysis of a SET domain PKMT with its intact polypeptide substrate.

Main Methods:

Cryo-electron microscopy was used to generate an 11-Å resolution density map of the Rubisco-RLSMT complex.
Atomic models were fitted into the density map using crystal structures of Rubisco and RLSMT.

Main Results:

The Rubisco-RLSMT complex exhibits extensive contact regions mediated by hydrophobic residues and leucine-rich repeats.
The structure provides insights into potential conformational changes during substrate binding and catalysis.

Conclusions:

This study presents the first structural insights into the interaction between RLSMT and its substrate, Rubisco.
The findings contribute to understanding the function of SET domain PKMTs in chloroplasts and their role in photosynthesis.