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Related Concept Videos

Covalently Linked Protein Regulators02:04

Covalently Linked Protein Regulators

Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
These groups modify specific amino acids in a protein.
Leaky Scanning02:28

Leaky Scanning

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 stands for...
Abnormal Proliferation02:23

Abnormal Proliferation

Under normal conditions, most adult cells remain in a non-proliferative state unless stimulated by internal or external factors to replace lost cells. Abnormal cell proliferation is a condition in which the cell's growth exceeds and is uncoordinated with normal cells. In such situations, cell division persists in the same excessive manner even after cessation of the stimuli, leading to persistent tumors. The tumor arises from the damaged cells that replicate to pass the damage to the daughter...
Initiation of Translation02:33

Initiation of Translation

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.
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RNA Stability01:53

RNA Stability

Intact DNA strands can be found in fossils, while scientists sometimes struggle to keep RNA intact under laboratory conditions. The structural variations between RNA and DNA underlie the differences in their stability and longevity. Because DNA is double-stranded, it is inherently more stable. The single-stranded structure of RNA is less stable but also more flexible and can form weak internal bonds. Additionally, most RNAs in the cell are relatively short, while DNA can be up to 250 million...
RNA Stability01:53

RNA Stability

Intact DNA strands can be found in fossils, while scientists sometimes struggle to keep RNA intact under laboratory conditions. The structural variations between RNA and DNA underlie the differences in their stability and longevity. Because DNA is double-stranded, it is inherently more stable. The single-stranded structure of RNA is less stable but also more flexible and can form weak internal bonds. Additionally, most RNAs in the cell are relatively short, while DNA can be up to 250 million...

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In situ Subcellular Fractionation of Adherent and Non-adherent Mammalian Cells
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Host cell sumoylation level influences papillomavirus E2 protein stability.

Yu-Chieh Wu1, Xue-Lin Bian, Phillip R Heaton

  • 1Department of Microbial and Molecular Pathogenesis, College of Medicine, Texas A&M Health Science Center, Reynolds Medical Building, College Station, TX 77843-1114, USA.

Virology
|March 3, 2009
PubMed
Summary

Papillomavirus E2 protein stability is enhanced by sumoylation, a modification that increases E2 protein levels in differentiating skin cells. This indirect stabilization mechanism links E2 protein expression to cellular differentiation.

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Area of Science:

  • Molecular Biology
  • Virology
  • Cell Biology

Background:

  • Papillomavirus E2 proteins are crucial for viral replication and are regulated by proteasomal degradation.
  • Sumoylation, a post-translational modification, is upregulated during keratinocyte differentiation.
  • Previous studies indicated a potential link between sumoylation and E2 protein stability.

Purpose of the Study:

  • To investigate whether sumoylation contributes to the stabilization of papillomavirus E2 proteins in differentiating keratinocytes.
  • To elucidate the mechanism by which sumoylation affects E2 protein levels.

Main Methods:

  • Assessing intracellular E2 protein amounts under conditions of altered sumoylation.
  • Measuring E2 protein transcript levels.
  • Determining the half-life of E2 proteins.
  • Performing in vitro studies to assess the effect of sumoylation on proteasomal degradation of E2 proteins.

Main Results:

  • Increased sumoylation led to higher intracellular levels of HPV E2 proteins (HPV11, 16, 18).
  • Sumoylation did not affect E2 protein transcript levels but significantly increased E2 protein half-life.
  • In vitro studies showed sumoylation blocks proteasomal degradation of the 16E2 protein, acting indirectly through cellular targets.

Conclusions:

  • Sumoylation-dependent, indirect stabilization of E2 proteins is a novel mechanism.
  • This process may link E2 protein levels to cellular differentiation and the cellular environment.
  • Papillomavirus E2 protein levels can be upregulated in differentiating keratinocytes due to increased sumoylation.