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Unlike eukaryotes, bacteria use a single RNA Polymerase (RNAP) to transcribe all genes. The different subunits of bacterial RNAPhave distinct functions. The multisubunit structure of the bacterial RNAP helps the enzyme to maintain catalytic function, facilitate assembly, interact with DNA and RNA, and self-regulate its activity.
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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.
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Nuclear protein sorting regulates nucleus composition and gene expression, crucial for determining the fate of a eukaryotic cell. Hence, the entry and exit of molecules across the nuclear envelope is a tightly controlled process. Nuclear protein sorting can be inhibited by one of the following ways: 1) masking cargo signal sequences, 2) modifying the nuclear receptor's affinity for cargo, 3) controlling the nuclear pore size, 4) retaining the cargo during its transit to the cytosol or the...
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Related Experiment Video

Updated: May 3, 2026

Measuring Transcellular Interactions through Protein Aggregation in a Heterologous Cell System
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RNase A does not translocate the alpha-hemolysin pore.

Besnik Krasniqi1, Jeremy S Lee1

  • 1Department of Biochemistry, University of Saskatchewan, Saskatoon, SK, Canada.

Plos One
|February 8, 2014
PubMed
Summary

This study investigated protein translocation through nanopores. Researchers found that ribonuclease A, despite interactions with the α-hemolysin pore, does not translocate it, challenging previous assumptions in nanopore sensing.

Area of Science:

  • Biophysics
  • Nanotechnology
  • Biochemistry

Background:

  • Nanopore sensing offers single-molecule protein analysis.
  • Direct evidence of protein translocation through the α-hemolysin pore is lacking.
  • Sensitive assays are needed to detect low numbers of translocating proteins.

Purpose of the Study:

  • To determine if proteins can translocate the α-hemolysin pore.
  • To develop a sensitive assay for protein translocation.
  • To investigate ribonuclease A interaction with the α-hemolysin pore.

Main Methods:

  • Utilized α-hemolysin nanopore sensing.
  • Developed a reverse transcription polymerase chain reaction (RT-PCR) based activity assay for ribonuclease A.
  • Analyzed ribonuclease A interactions under varying experimental conditions (voltage, denaturants).

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Main Results:

  • Ribonuclease A induced blockade events in the α-hemolysin pore.
  • Ribonuclease A exhibited charge reversal under experimental conditions.
  • No ribonuclease A activity was detected in the trans chamber, indicating no translocation.

Conclusions:

  • Ribonuclease A does not translocate the α-hemolysin pore.
  • Observed blockade events were not due to translocation.
  • Further research is needed to establish direct evidence of protein translocation via nanopores.