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From Proteopedia
genetics is ok
'Molecules it Interacts With and where '
The protein binds to GDP as well as the following ligands in order to promote the attachment of the protein complex to the ribosome A site.
PHOSHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER
PHENYLALANINE
MAGNESIUM ION
'Origin'
It has domains that are created in yeast (phenyl-transfer RNA) , in the heat resistant Thermus aquaticus (EF-Tu elongation factor, and can be synthetically manufactured.
'Structure'
It has 3 domains. G proteins, Elongation Factors, and the EF-Tu/eEF-1alpha/eIF2-gamma C-terminal domain. It is composed of 6 chains, which combine in alignment.
Specific are highlighted here. The ligands listed above, GDP, Phe, and Mg+2 ion each attach at these locations which are still being explored.
which play a crucial role in binding to the ribosome during translation. They form positive pockets with which negative amino acids can bind to.
'Molecules it Interacts With and where '
The protein binds to GDP as well as the following ligands in order to promote the attachment of the protein complex to the ribosome A site.
PHOSHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER
PHENYLALANINE
MAGNESIUM ION
'Origin'
It has domains that are created in yeast (phenyl-transfer RNA) , in the heat resistant Thermus aquaticus (EF-Tu elongation factor, and can be synthetically manufactured.
'Structure'
It has 3 domains. G proteins, Elongation Factors, and the EF-Tu/eEF-1alpha/eIF2-gamma C-terminal domain. It is composed of 6 chains, which combine in alignment.
Specific are highlighted here.
which play a crucial role in binding to the ribosome during translation.
'Function"
The protein complex participates in placing the amino acids in their correct order when messenger RNA is translated into a protein sequence on the ribosome by promoting GTP-dependent binding of tRNA to the A site of the ribosome. In other words, it is involved with elongation during polypeptide synthesis.
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Connor McDermott and Niall Cope's Structure: E.coli RNA Polymerase sigma-70 Holoenzyme
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Functions
The RNA Polymerase sigma-70 Holoenzyme is crucial in the initiation stage of transcription. First, regular RNA polymerase binds to the sigma factor, sigma-70, upon recognition of the promoter consenus sequence the RNA polymerase holoenzyme attaches to the DNA template strand at the promoter region. After this initiation phase, RNA Polymerase sigma-70 holoenzyme catalyzes elongation, then like a caterpillar, the holoenzyme breaks down only to have a beautiful, strong, transcribing RNA Polymerase born from the tattered shell of the holoenzyme.
What it interacts with
The sigma factor alters the chemical structure of the RNA polymerase, allowing the RNA polyermase to bind to the promoter region, beginning the process of elongation. So, the holoenzyme primarily interacts with the DNA template and the nucleotides of the mRNA.
Where it Interacts
Since DNA is in the nucleus, and the holoenzyme interacts with DNA, it's obviously interacting in the golgi apparatus. No, the interaction between the holoenzyme and the DNA happens in the nucleus, specifically the promoter region.
What Organism is E.Coli RNA Polymerase Sigma-70 Holoenzyme located in?
Some would say E.coli, they would be right.
Diseases
E. Coli is associated with several lit bacterial infections like: cholecystitis (gallbladder infection), bactermia (bacterial infection in the blood), cholangitis (infection of the liver bile ducts), UTIs, traveler's diarrhea (can strike at home), and meningitis.
Relevance
E.Coli is a crucial part of the human digestive system, helping breakdown complex macromolecules. E. Coli is also responsible for several bacterial infections, which is particularly relevant to travelers, see [1] and scroll down.
Structural highlights
The RNA Polymerase Sigma-70 Holoenzyme has twelve different different protein groups. However, the interaction of the protein is based on the structure of the subunits. Highlighted in red is the of this RNA polymerase, highlighted in blue is the of this RNA polymerase, and highlighted in magenta is the of this RNA polymerase. Another crucial aspect of protein interactions is the secondary protein folding, highlighted in
Fun Facts
Most studied bacterial RNA polymerase. Donald's favorite bacterial RNA polymerase. Sigma factor 70 is the primary sigma factor of the E.coli.
