Modomics - A Database of RNA Modifications
RNA (guanine-7-)methyltransferase, the enzyme responsible for methylating the 5 cap structure of eukaryotic mRNA, was isolated from extracts of Saccharomyces cerevisiae. The yeast enzyme catalyzed methyl group transfer from S-adenosyl-L-methionine to the guanosine base of capped, unmethylated poly(A). Cap methylation was stimulated by low concentrations of salt and was inhibited by S-adenosyl-L-homocysteine, a presumptive product of the reaction, but not by S-adenosyl-D-homocysteine. The methyltransferase sedimented in a glycerol gradient as a single discrete component of 3.2S. A likely candidate for the gene encoding yeast cap methyltransferase was singled out on phylogenetic grounds. The ABD1 gene, located on yeast chromosome II, encodes a 436-amino-acid (50-kDa) polypeptide that displays regional similarity to the catalytic domain of the vaccinia virus cap methyltransferase. That the ABD1 gene product is indeed RNA (guanine-7-)methyltransferase was established by expressing the ABD1 protein ...
Eukarys C3P3 expression system - Eukarys
Previously, the in vitro production of mRNA was limited in yield and translational activity by the co-transcriptional capping method using cap analog.The presence of dinucleotide cap analog in the transcription reaction mix greatly decreases the mRNA yields and inhibits translation when non-incorporated dinucleotide analogs are not carefully removed. Instead of using a costly and inefficiently incorporated nucleotide cap analog, the C3P3® mRNA Production System uses a virus-derived capping enzyme physically coupled to the RNA polymerase to add the cap at high efficiency capping - versus 80% for other systems using standard m7GpppG cap analog or anti-reverse cap analog (ARCA) and 100% proper cap orientation. The standard cap analog (m7GpppG) used in co-transcriptional reactions can be incorporated in the reverse orientation (33-50% of the time) which is not translated in the cell, thereby decreasing the amount of protein produced per microgram of transfected mRNA.. Simultaneously, the capped ...
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The role of 5 -leader length, secondary structure and PABP concentration on cap and poly(A) tail function during translation...
The 5-cap structure and poly(A) tail of eukaryotic mRNAs function synergistically to promote translation initiation through a physical interaction between the proteins that bind to these regulatory elements, In this study, we have examined the effect of leader length and the presence of secondary structure on the translational competence and the function of the cap and poly(A) tail for mRNAs microinjected into Xenopus oocytes, Increasing the length of the 5-leader from 17 to 144 nt resulted in a 2- to 4-fold increase in expression from an mRNA containing an unstructured leader but increased expression up to 20-fold for an mRNA containing 5-proximal structure. Consequently, the presence of secondary structure was less inhibitory for those mRNAs with a longer 5-leader. Go-injection of poly(A)-binding protein (PABP) mRNA increased the function of the cap and poly(A) tail in promoting translation from poly(A)(+) but not poly(A)(-) mRNAs, particularly for mRNAs containing secondary structure. In ...
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A common structural feature of all cellular eukaryotic mRNAs (except for organelle mRNAs) analyzed to date is the presence of a 5′-terminal m7GpppN (where N is any nucleotide) structure, termed the cap (140). This structure is added early during RNA polymerase II-driven transcription and is required for several steps of mRNA biogenesis. Consistent with the diverse roles of the cap during gene expression, a number of cap binding proteins have been identified in the cytoplasm and nucleus (54, 140). The first-described, and best-characterized of these, is eukaryotic initiation factor-4E (eIF-4E), a 24-kDa polypeptide that has been cloned and characterized from a number of species. This protein shows strong binding specificity for methylated, cap structures of eukaryotic mRNAs (54).. We have developed an affinity chromatography procedure, called CAPture, that allows for the purification of mRNA via the cap structure (44). Previous to this, several laboratories had used antibodies directed against ...
Novel Cytoplasmic Cap Binding Proteins in Yeast | Springer for Research & Development
The 5′ terminal cap structure, m7GpppX (where X is any nucleotide), is a ubiquitous feature of eukaryotic mRNAs that plays an important role in the cytoplasm and the nucleus. In the cytoplasm the cap...
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EC 3.6.1 and EC 3.6.2
EC 3.6.1.59 Accepted name: 5-(N7-methyl 5-triphosphoguanosine)-[mRNA] diphosphatase. Reaction: a 5-(N7-methyl 5-triphosphoguanosine)-[mRNA] + H2O = N7-methylguanosine 5-phosphate + a 5-diphospho-[mRNA]. Other name(s): DcpS; m7GpppX pyrophosphatase; m7GpppN m7GMP phosphohydrolase; m7GpppX diphosphatase; m7G5ppp5N m7GMP phosphohydrolase. Systematic name: 5-(N7-methyl 5-triphosphoguanosine)-[mRNA] N7-methylguanosine 5-phosphate phosphohydrolase. Comments: The enzyme removes (decaps) the N7-methylguanosine 5-phosphate cap from an mRNA degraded to a maximal length of 10 nucleotides [3,6]. Decapping is an important process in the control of eukaryotic mRNA degradation. The enzyme functions to clear the cell of cap structure following decay of the RNA body [2]. The nematode enzyme can also decap triply methylated substrates, 5-(N2,N2,N7-trimethyl 5-triphosphoguanosine)-[mRNA] [4].. Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: References:. 1. Malys, N. and ...
Ribo m7G Cap Analog
This methylated ribonucleotide can be incorporated onto the 5´-end of in vitro transcripts and simulates the cap structure found on most eukaryotic mRNA molecules.
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statistics - Given that the system works, compute the probability that component is working. - Mathematics Stack Exchange
Because component failures are independent: $$\begin{align}\mathsf P(B\mid A\cap (B\cup C)\cap D) ~=~& \dfrac{\mathsf P(B\cap A\cap (B\cup C)\cap D)}{\mathsf P(A\cap(B\cup C)\cap D)} \\=~& \dfrac{\mathsf P(A\cap B\cap D)}{\mathsf P(A\cap(B\cup C)\cap D)} \\=~& \dfrac{\mathsf P(A)~\mathsf P( B)~\mathsf P( D)}{\mathsf P(A)~\mathsf P(B\cup C)~\mathsf P(D)} \\=~& \dfrac{\mathsf P(B)}{\mathsf P(B\cup C)} &\bbox[ghostwhite]{\color{ghostwhite}{=~\dfrac{\mathsf P(B)}{\mathsf P(B)+\mathsf P(C)-\mathsf P(B)~\mathsf P(C)}}}\\=~&\dfrac{\mathsf P(B\cap(B\cup C))}{\mathsf P(B\cup C)} \\[2ex]\therefore \mathsf P(B\mid A\cap (B\cup C)\cap D) ~=~& \mathsf P(B\mid B\cup C)\end{align}$$. ...
Repression of oncogenic cap-mediated translation by 4Ei-10 diminishes proliferation, enhances chemosensitivity and alters...
Activated cap-dependent translation promotes cancer by stimulating translation of mRNAs encoding malignancy-promoting proteins. The nucleoside monophosphat
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Safety, Sample Integrity and Throughput With Semi-Automated Sample Tube Decapping
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docs/man1.1.0/man3/OPENSSL ia32cap.html
For example, in 32-bit application context clearing bit #26 at run-time disables high-performance SSE2 code present in the crypto library, while clearing bit #24 disables SSE2 code operating on 128-bit XMM register bank. You might have to do the latter if target OpenSSL application is executed on SSE2 capable CPU, but under control of OS that does not enable XMM registers. Historically address of the capability vector copy was exposed to application through OPENSSL_ia32cap_loc(), but not anymore. Now the only way to affect the capability detection is to set OPENSSL_ia32cap environment variable prior target application start. To give a specific example, on Intel P4 processor env OPENSSL_ia32cap=0x16980010 apps/openssl, or better yet env OPENSSL_ia32cap=~0x1000000 apps/openssl would achieve the desired effect. Alternatively you can reconfigure the toolkit with no-sse2 option and recompile.. Less intuitive is clearing bit #28, or ~0x10000000 in the environment variable terms. The truth is ...
troubles with caps
One more question along these lines, actually: does caps_sys_wait() :block the entire process or just the current pthread? : :-Chris Actually theres an issue there. The CAPS id is associated with a thread so only the pthread that opened the CAPS connection has access to it. In anycase, caps_sys_wait() will only block the pthread because our pthreads implementation is rfork based. -Matt Matthew Dillon ,dillon at xxxxxxxxxxxxx ...
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Patent US6370206 - Adaptive cap receiver and method for controlling a cap receiver - Google Patents
An adaptive CAP filter includes a clock-controlled A/D converter for converting an input signal, a digital level-control circuit, an adaptive controlled reception filtering system with two parallel filters and a downstream decision maker for outputting reconstructed signal coordinates. The digital level-control circuit and the adaptive reception filtering system are decoupled by virtue of the fact that either an adjustment of the digital level-control circuit or a coefficient adjustment of the adaptive reception filtering system is active. A method for controlling a cap receiver is also provided.
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