rna-dependent rna polymerase

SARS-CoV-2 RNA-dependent RNA polymerase RDRP Protein (His) is expressed in Baculovirus insect cells with His tag. The predicted molecular weight is 108.3 kDa and the accession number is YP_009725307.1.

Highly processive DNA-dependent RNA polymerase that catalyzes the transcription of class II and class III viral genes. Recognizes a specific promoter sequence and enters first into an 'abortive phase' where very short transcripts are synthesized and released before proceeding to the processive transcription of long RNA chains. Unwinds the double-stranded DNA to expose the coding strand for templating. Participates in the initiation of viral DNA replication presumably by making primers accessible to the DNA polymerase, thus facilitating the DNA opening. Plays also a role in viral DNA packaging, probably by pausing the transcription at the right end of concatemer junction to allow packaging complex recruitment and beginning of the packaging process.

Chaperone protein required for seedling and chloroplast development under heat stress, probably by maintaining plastid-encoded RNA polymerase (PEP)-dependent transcription. HSP21, chloroplastic Protein, Arabidopsis thaliana, Recombinant (His & Myc) is expressed in E. coli expression system with N-10xHis and C-Myc tag. The predicted molecular weight is 28.4 kDa and the accession number is P31170.

NSP8 is a nonstructural protein of coronavirus. NSP8 acts as a primase in RNA synthesis. NSP8 and NSP7 are essential co-factors of NSP12 (the catalytic subunit with RNA-dependent RNA polymerase activity) that can remarkably stimulate RdRp activity. The nsp12-nsp7-nsp8 subcomplex is defined as the minimal core component for mediating coronavirus RNA synthesis. SARS-CoV-2 NSP8 Protein is expressed in E. coli expression system. The predicted molecular weight is 22.04 kDa and the accession number is YP_009725304.1.

One of two assembly initiator proteins for the 30S subunit, it binds directly to 16S rRNA where it nucleates assembly of the body of the 30S subunit.; With S5 and S12 plays an important role in translational accuracy; many suppressors of streptomycin-dependent mutants of protein S12 are found in this protein, some but not all of which decrease translational accuracy (ram, ribosomal ambiguity mutations).; Plays a role in mRNA unwinding by the ribosome, possibly by forming part of a processivity clamp.; Protein S4 is also a translational repressor protein, it controls the translation of the alpha-operon (which codes for S13, S11, S4, RNA polymerase alpha subunit, and L17) by binding to its mRNA.; Also functions as a rho-dependent antiterminator of rRNA transcription, increasing the synthesis of rRNA under conditions of excess protein, allowing a more rapid return to homeostasis. Binds directly to RNA polymerase.; Part of the processive rRNA transcription and antitermination complex (rrnTAC). The complex forms an RNA-chaperone ring around the RNA exit tunnel of RNA polymerase (RNAP). It supports rapid transcription and antitermination of rRNA operons, cotranscriptional rRNA folding, and annealing of distal rRNA regions to allow correct ribosome biogenesis. This subunit may play a particular role in long-distance rRNA annealing needed for pre-rRNA processing.

DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Common component of RNA polymerases I, II and III which synthesize ribosomal RNA precursors, mRNA precursors and many functional non-coding RNAs, and small RNAs, such as 5S rRNA and tRNAs, respectively. Pol II is the central component of the basal RNA polymerase II transcription machinery. Pols are composed of mobile elements that move relative to each other. In Pol II, RPB5 is part of the lower jaw surrounding the central large cleft and thought to grab the incoming DNA template. Seems to be the major component in this process.

Stimulates translation by blocking the activation of the dsRNA-dependent protein kinase EIF2AK2 PKR, thereby inhibiting the host interferon response. Sigma3 prevents the activation of EIF2AK2 by competing with the kinase for dsRNA-binding.; The viral outer shell polypeptides, of which sigma-3 is one, impose structural constraints that prevent elongation of nascent transcripts by the RNA-dependent RNA polymerase lambda-3. Reovirus type 3 (strain Dearing) Outer capsid protein sigma-3 (His) is expressed in E. coli expression system with N-6xHis tag. The predicted molecular weight is 45.2 kDa and the accession number is P03527.

Cleavage by the viral main protease, 3CLpro results in generating the nsp8 protein, The nsp8 protein has been shown to associate with several other nsps and to colocalize with these nsps in cytoplasmic complexes that are important for viral RNA synthesis. It forms a hexadecamer with nsp7 (8 subunits of each) that may participate in viral replication by acting as a primase. Alternatively, may synthesize substantially longer products than oligonucleotide primers.Nsp8 was shown to have RNA-dependent RNA polymerase (RdRp) activity that could be involved in producing primers utilized by nsp12 which is normally accepted to be the RdRp for SARS-CoV.

3C-like protease (3CLpro) is the main protease of Humann Coronavirus. 3C-like protease (3CLpro) is a key enzyme, as it cleaves several sites to produce non-structural proteins that are essential for genome replication and Coronavirus virion production, such as an RNA-dependent RNA polymerase, a helicase, ribonucleases and 3CLpro itself, from two types of polyproteins (pp1a and pp1ab). SARS-CoV 3CLpro exists as a homodimer and each protomer has an active site. SARS-CoV-2 3CLpro 3C-like protease Protein (His & Avi) is expressed in E. coli expression system. The predicted molecular weight is 36.57 kDa and the accession number is YP_009725295.1.

Zika virus NS5 is involved in methytransferase and RNA guanylytransferase activities and capping and synthesis of RNA. And, NS5 is also an RNA-dependent RNA polymerase.

3C-like protease (3CLpro) is the main protease of Humann Coronavirus. 3C-like protease (3CLpro) is a key enzyme, as it cleaves several sites to produce non-structural proteins that are essential for genome replication and Coronavirus virion production, such as an RNA-dependent RNA polymerase, a helicase, ribonucleases and 3CLpro itself, from two types of polyproteins (pp1a and pp1ab). SARS-CoV 3CLpro exists as a homodimer and each protomer has an active site. SARS-CoV-2 3CLpro 3C-like protease Protein (His) is expressed in Baculovirus insect cells. The predicted molecular weight is 35.31 kDa and the accession number is YP_009725295.1.

DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Component of RNA polymerase III which synthesizes small RNAs, such as 5S rRNA and tRNAs. Plays a key role in sensing and limiting infection by intracellular bacteria and DNA viruses. Acts as nuclear and cytosolic DNA sensor involved in innate immune response. Can sense non-self dsDNA that serves as template for transcription into dsRNA. The non-self RNA polymerase III transcripts, such as Epstein-Barr virus-encoded RNAs (EBERs) induce type I interferon and NF- Kappa-B through the RIG-I pathway.

Rna-dependent RNA polymerase part of the packaging complex that packages the viral RNA segments, replicate them into a double-stranded form and transcribe them. P2 Protein, Pseudomonas phage phi6, Recombinant (His & Myc) is expressed in E. coli expression system with N-10xHis and C-Myc tag. The predicted molecular weight is 27.2 kDa and the accession number is P11124.

DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Largest and catalytic core component of RNA polymerase III which synthesizes small RNAs, such as 5S rRNA and tRNAs. Forms the polymerase active center together with the second largest subunit. A single-stranded DNA template strand of the promoter is positioned within the central active site cleft of Pol III. A bridging helix emanates from RPC1 and crosses the cleft near the catalytic site and is thought to promote translocation of Pol III by acting as a ratchet that moves the RNA-DNA hybrid through the active site by switching from straight to bent conformations at each step of nucleotide addition. Plays a key role in sensing and limiting infection by intracellular bacteria and DNA viruses. Acts as nuclear and cytosolic DNA sensor involved in innate immune response. Can sense non-self dsDNA that serves as template for transcription into dsRNA. The non-self RNA polymerase III transcripts, such as Epstein-Barr virus-encoded RNAs (EBERs) induce type I interferon and NF- Kappa-B through the RIG-I pathway.

SIRT1 belongs to the sirtuin family. Members of the sirtuin family are characterized by a sirtuin core domain and grouped into four classes. SIRT1 is included in class I of the sirtuin family. It is a NAD-dependent protein deacetylase, which regulates processes such as apoptosis and muscle differentiation by deacetylating key proteins. It deacetylates 'Lys-382' of p53 TP53 and impairs its ability to induce proapoptotic program and modulate cell senescence. SIRT1 also deacetylates TAF1B and thereby represses rDNA transcription by the RNA polymerase I. It is involved in HES1- and HEY2-mediated transcriptional repression. SIRT1 inhibits skeletal muscle differentiation by deacetylating PCAF and MYOD1. It may serve as a sensor of the cytosolic ratio of NAD(+) NADH, which is essential in skeletal muscle cell differentiation. It also deacetylates 'Lys-16' of histone H4 (in vitro). Component of the eNoSC (energy-dependent nucleolar silencing) complex, a complex that mediates silencing of rDNA in response to intracellular energy status and acts by recruiting histone-modifying enzymes. The eNoSC complex is able to sense the energy status of cell: upon glucose starvation, elevation of NAD(+) NADP(+) ratio activates SIRT1, leading to histone H3 deacetylation followed by dimethylation of H3 at 'Lys-9' (H3K9me2) by SUV39H1 and the formation of silent chromatin in the rDNA locus.

NSP8 is a nonstructural protein of coronavirus. NSP8 acts as a primase in RNA synthesis. NSP8 and NSP7 are essential co-factors of NSP12 (the catalytic subunit with RNA-dependent RNA polymerase activity) that can remarkably stimulate RdRp activity. The nsp12-nsp7-nsp8 subcomplex is defined as the minimal core component for mediating coronavirus RNA synthesis. SARS-CoV-2 NSP8 Protein (Avi) is expressed in E. coli expression system. The predicted molecular weight is 24.17 kDa and the accession number is YP_009725304.1.