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

Co-activators and Co-repressors

Co-activators and Co-repressors

Gene transcription is regulated by the synergistic action of several proteins that form a complex at a gene regulatory site. This is observed in eukaryotes, where the regulation of gene expression is a complex process. Regulatory proteins in eukaryotes can broadly be classified into two types – regulators that bind directly to specific DNA sequences and co-regulators that associate with regulatory proteins but cannot directly bind to the DNA. These co-regulators are further divided into...

Co-activators and Co-repressors

Co-activators and Co-repressors

Gene transcription is regulated by the synergistic action of several proteins that form a complex at a gene regulatory site. This is observed in eukaryotes, where the regulation of gene expression is a complex process. Regulatory proteins in eukaryotes can broadly be classified into two types – regulators that bind directly to specific DNA sequences and co-regulators that associate with regulatory proteins but cannot directly bind to the DNA. These co-regulators are further divided into...

Alternative RNA Splicing

Alternative RNA Splicing

Alternative RNA splicing is the regulated splicing of exons and introns to produce different mature mRNAs from a single pre-mRNA. Unlike in constitutive splicing where a single gene produces a single type of mRNA, alternative splicing allows an organism to produce multiple proteins from a single gene and plays an important role in protein diversity.
There are five types of alternative RNA splicing that vary in the ways the pre-mRNA segments are removed or retained in the mature mRNA. The first...

RNA Polymerase II Accessory Proteins

RNA Polymerase II Accessory Proteins

Proteins that regulate transcription can do so either via direct contact with RNA Polymerase or through indirect interactions facilitated by adaptors, mediators, histone-modifying proteins, and nucleosome remodelers. Direct interactions to activate transcription is seen in bacteria as well as in some eukaryotic genes. In these cases, upstream activation sequences are adjacent to the promoters, and the activator proteins interact directly with the transcriptional machinery. For example, in...

RNA Polymerase II Accessory Proteins

RNA Polymerase II Accessory Proteins

Proteins that regulate transcription can do so either via direct contact with RNA Polymerase or through indirect interactions facilitated by adaptors, mediators, histone-modifying proteins, and nucleosome remodelers. Direct interactions to activate transcription is seen in bacteria as well as in some eukaryotic genes. In these cases, upstream activation sequences are adjacent to the promoters, and the activator proteins interact directly with the transcriptional machinery. For example, in...

Prokaryotic Transcriptional Activators and Repressors

Prokaryotic Transcriptional Activators and Repressors

The organization of prokaryotic genes in their genome is notably different from that of eukaryotes. Prokaryotic genes are organized, such that the genes for proteins involved in the same biochemical process or function are located together in groups. This group of genes, along with their regulatory elements, are collectively known as an operon. The functional genes in an operon are transcribed together to give a single strand of mRNA known as polycistronic mRNA.
Transcription of prokaryotic...

You might also read

Related Articles

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

Sort by

Same author

Enhancer RNAs: similarities with both lncRNAs and mRNAs reveal novel functions.

RNA biology·2026

Same author

Multiple human enhancer RNAs contain long translated open reading frames.

Genes & development·2025

Same author

SUGP1 loss drives SF3B1 hotspot mutant missplicing in cancer.

Cell reports·2025

Same author

Multiple human enhancer RNAs contain long translated open reading frames.

bioRxiv : the preprint server for biology·2025

Same author

Cancer-associated SF3B1 mutation K700E causes widespread changes in U2/branchpoint recognition without altering splicing.

Proceedings of the National Academy of Sciences of the United States of America·2025

Same author

Protocol for detection of cGAMP-induced STING oligomerization in cultured cells.

STAR protocols·2025

Search research articles

Related Experiment Video

Updated: Jul 1, 2026

Exploring Sequence Space to Identify Binding Sites for Regulatory RNA-Binding Proteins

Exploring Sequence Space to Identify Binding Sites for Regulatory RNA-Binding Proteins

Published on: August 9, 2019

Phosphorylation switches the general splicing repressor SRp38 to a sequence-specific activator.

Ying Feng¹, Mo Chen, James L Manley

¹Department of Biological Sciences, Columbia University, 1212 Amsterdam Avenue, New York, New York 10027, USA.

Nature Structural & Molecular Biology

|September 17, 2008

Summary

Phosphorylated SRp38 acts as a sequence-specific splicing activator, unlike its repressor role when dephosphorylated. This atypical SR protein requires a cofactor for full activity, influencing spliceosome complex formation and pre-mRNA recognition.

More Related Videos

Engineering Artificial Factors to Specifically Manipulate Alternative Splicing in Human Cells

Engineering Artificial Factors to Specifically Manipulate Alternative Splicing in Human Cells

Published on: April 26, 2017

Using the E1A Minigene Tool to Study mRNA Splicing Changes

Using the E1A Minigene Tool to Study mRNA Splicing Changes

Published on: April 22, 2021

Related Experiment Videos

Last Updated: Jul 1, 2026

Exploring Sequence Space to Identify Binding Sites for Regulatory RNA-Binding Proteins

Exploring Sequence Space to Identify Binding Sites for Regulatory RNA-Binding Proteins

Published on: August 9, 2019

Engineering Artificial Factors to Specifically Manipulate Alternative Splicing in Human Cells

Engineering Artificial Factors to Specifically Manipulate Alternative Splicing in Human Cells

Published on: April 26, 2017

Using the E1A Minigene Tool to Study mRNA Splicing Changes

Using the E1A Minigene Tool to Study mRNA Splicing Changes

Published on: April 22, 2021

Area of Science:

Molecular Biology
RNA Splicing
Gene Regulation

Background:

SRp38 is an atypical SR protein known to function as a general splicing repressor in its dephosphorylated state.
The precise mechanisms and alternative functions of SRp38 in gene regulation remain incompletely understood.

Purpose of the Study:

To investigate the function of phosphorylated SRp38 in RNA splicing.
To elucidate the mechanism by which SRp38 influences spliceosome assembly and activity.
To determine if SRp38 can act as a sequence-specific splicing activator.

Main Methods:

Biochemical assays to study splicing complex formation.
Analysis of SRp38 cofactor requirements.
Investigation of SRp38's effect on U1 and U2 snRNP binding to pre-mRNA.
Examination of SRp38's role in the alternative splicing of glutamate receptor B pre-mRNA.

Main Results:

Phosphorylated SRp38 functions as a sequence-specific splicing activator.
SRp38 requires a cofactor for its activator function, but can induce early spliceosomal complex A formation independently.
The cofactor is essential for the progression to spliceosomal complexes B and C.
SRp38 enhances the stable recognition of pre-mRNA by U1 and U2 snRNPs.
SRp38 specifically alters the splicing pattern of glutamate receptor B pre-mRNA.

Conclusions:

SRp38 exhibits a dual role in RNA splicing, acting as both a repressor and an unusual sequence-specific activator.
The phosphorylation state of SRp38 dictates its function in splicing.
SRp38's activator function relies on a cofactor and impacts spliceosome assembly and substrate recognition.