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Related Concept Videos

pre-mRNA Processing02:01

pre-mRNA Processing

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In eukaryotic cells, transcripts made by RNA polymerase are modified and processed before exiting the nucleus. Unprocessed RNA is called precursor mRNA or pre-mRNA to distinguish it from mature mRNA.
Once about 20-40 ribonucleotides have been joined together by RNA polymerase, a group of enzymes adds a “cap” to the 5’ end of the growing transcript. In this process, a 5’ phosphate is replaced by modified guanosine that has a methyl group attached to it (7-Methyl...
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Directing Proteins to the Rough Endoplasmic Reticulum01:34

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The organelle-specific signaling sequences direct proteins synthesized in the cytosol to their final destination like ER, mitochondria, peroxisomes, etc. Some of the proteins directed to ER are then trafficked via vesicles to other organelles within the cell or the extracellular environment through the Golgi complex. For example, the rough ER synthesizes soluble proteins for transportation to the lysosomes or secretion out of the cell. It can also synthesize transmembrane proteins that can...
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Pre-mRNA Processing: Modification of pre-mRNA Ends01:35

Pre-mRNA Processing: Modification of pre-mRNA Ends

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In eukaryotic cells, transcripts made by RNA polymerase are modified and processed before exiting the nucleus. Unprocessed RNA is called precursor mRNA or pre-mRNA to distinguish it from mature mRNA.
Once about 20-40 ribonucleotides have been joined together by RNA polymerase, a group of enzymes adds a cap to the 5' end of the growing transcript. In this process, a 5' phosphate is replaced by modified guanosine that has a methyl group attached (7-methyl guanosine). This 5' cap helps...
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Post-translational Translocation of Proteins to the RER01:27

Post-translational Translocation of Proteins to the RER

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A sizable fraction of proteins destined for ER are first synthesized in the cell cytosol and then transported across the ER membrane–a process called post-translational translocation. Similar to cotranslationally translocated proteins, these proteins also use the Sec translocon complex to enter the ER lumen.
Targeting proteins to the ER
Hsp40 and Hsp70 chaperone molecules bind the translated proteins in the cytosol to prevent their folding. The chaperone binding helps to keep the signal...
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Leaky Scanning02:28

Leaky Scanning

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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...
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Pre-mRNA Processing: RNA Splicing01:36

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Related Experiment Video

Updated: Dec 31, 2025

Single-step Purification of Macromolecular Complexes Using RNA Attached to Biotin and a Photo-cleavable Linker
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SYNCRIP, a new player in pri-let-7a processing.

Ying Chen1, Jingru Chan1, Wei Chen1

  • 1Department of Biological Sciences and Centre for Bioimaging Sciences, National University of Singapore, Singapore 117543, Singapore.

RNA (New York, N.Y.)
|January 8, 2020
PubMed
Summary

SYNCRIP protein is identified as a novel cofactor that regulates let-7a microRNA biogenesis. This discovery offers new insights into miRNA regulation and its role in eukaryotic development.

Keywords:
SYNCRIPmiRNA biogenesispri-let-7a processing

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PAR-CliP - A Method to Identify Transcriptome-wide the Binding Sites of RNA Binding Proteins

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Area of Science:

  • Molecular Biology
  • Gene Regulation
  • Biochemistry

Background:

  • MicroRNAs (miRNAs) are endogenous molecules regulating gene expression.
  • Factors influencing let-7 miRNA biogenesis are known, but more auxiliary factors require investigation.

Purpose of the Study:

  • To identify novel auxiliary factors involved in let-7a miRNA biogenesis.
  • To elucidate the mechanism by which SYNCRIP regulates let-7a miRNA.

Main Methods:

  • In vivo and in vitro interaction studies between SYNCRIP and pri-let-7a.
  • Knockdown and overexpression experiments of SYNCRIP.
  • miRNA profiling analysis.
  • Association studies with the microprocessor complex.
  • Functional analysis of SYNCRIP domains.

Main Results:

  • SYNCRIP interacts with pri-let-7a and regulates let-7a expression.
  • SYNCRIP associates with the microprocessor complex, promoting pri-let-7a processing.
  • The terminal loop of pri-let-7a is crucial for SYNCRIP interaction.
  • The RRM2-3 domain of SYNCRIP promotes pri-let-7a processing.

Conclusions:

  • SYNCRIP is a novel regulator of let-7a miRNA biogenesis.
  • SYNCRIP plays a significant role in miRNA regulation and eukaryotic development.