translation

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How is the order of nucleotides in mRNA used to generate the linear sequences of amino acids in protein?

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What process is the most highly conserved across all organism and the most energetically costly?

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Transcription is a more formidable challenge than translation.

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The hydrophobic side chains of phenylalanine, tyrosine, and tryptophan forms interactions with the mRNA template.

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Crick proposed a molecule that directly interacts with the coding units of mRNA. He proposed to also be a molecule.

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amino acids that are attached to a class of RNA molecules that represent 15% of all celluar RNA and transfer amino acids to a growing polypeptide chain.

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The translation machinery is comprised of ?

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The competent of the translation machinery are always discarded after use.

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Provides the information to be interpreted by translation machinery

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This region of the mRNA specifies the order of amino acids by the ordered series of 3-nucleotide-long units called codons?

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couple amino acids to specific tRNAs that recognize the appropriate codon?

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coordinates correct recognition of mRNA by each tRNA and catalyzes peptide bond formation between growing peptide chain and amino acids attached to tRNA

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in mRNA containing 2 or more open reading frames that can encode for multiple polypeptide chains

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protein coding regions of each mRNA is composed of contiguous, non-overlapping string of codons called?

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Eukaryotes, contain a single ORF that encode for multiple protein which is called polycistronic.

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translation starts at the ❌ end of ORF and proceeds into the 3' end

5'

3'

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Start codons in bacteria

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eukaryotic cells always use AUG as a stop codon

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fundamental unit of an ORF is a

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What are the important functions of a start codon?

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Since the codons are a 3-nucleotide long, any stretch of mRNA could be translated in three different reading frames by overlapping.

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Stop codons are UAG,UGA and UAA in both eukaryotes and prokaryotes

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Eukaryotic mRNA recruit ribosomes by the shine-dalgarno sequence which is ribosome binding site(RBS) that recruit the translation machinery.

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the ribosome binding site

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limited complementarity and poor spacing promotes active translation

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some prokaryotes lack a strong RBS but can still be actively translated by having a start and a stop codon right next to each other.

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who uses their 5' and 3' modified ends to facilitate translation?

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Kozak sequence

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5' cap allows the ribosome to be recruited in order to go through a process called scanning.

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at the end of mRNA enhances the level of translation of mRNA by promoting efficient recycling of .

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molecules are 75 to 95 ribonucleotides in length which there are many types of.

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The site at which amino acid is attached by the enzyme aminoacyl tRNA syntheses?

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Unusual bases found in tRNAs primary structure created by post-transcriptional modifications?

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principle features of the tRNA clover leaf are

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L-shape reveals the secondary structure of tRNA, which is stabilized by hydrogen bonds only.

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charged tRNAs have an amino acid attached to them by amino alkyl linkage

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acyl linkage is a high energy bond that is hydrolysis results in a large change in free energy, which helps drive the formation of peptide bonds

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step one of aminoacyl-tRNA charging is which amino acid reacts with ATP, amino acid is attached to adenylic acid via group transfer ester bond.

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Whats the driving force that make adenylaltion energetically favorable reaction?

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In step two of aminoacyl tRNA-charging- the adenylylated amino acid which is highly bound to the synthetase reacts with?

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Class 2 tRNA syntheses enzyme attach the amino acid to the 2'OH of the tRNA and are generally monomeric.

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each aminoacyl tRNA synthetase attaches a single amino acid to only one tRNA which is know as isoaccepting tRNAs.

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most organism have 20 different tRNA synthetase

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tRNA structure that determine recognition by specific aminacyl tRNA synthetases?

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Why does aminoacyl-tRNA synthetase face a challenge in selecting the correct amino acid?

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There is more proofreading after the aminoacyl-tRNA synthetase has used its editing pocket to charge tRNAs with low accuracy.

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when cysteinyl-tRNA ^cys converted to alanine-tRNA^ cys ( by reduction) and added to a cell free protein synthesizing system, alanine-tRNA^cys introduces alanines at the codons that are suppose to be cysteine. why?

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Eukaryotes can commence translation of the mRNA as it emerges from the RNA polymerase because the transcription machinery and the translation machinery are in the same compartment.

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The ribosome is made up of large subunit which contains the ❌ and the small subunit that contains the ❌.

decoding center

peptidase transferase center

30S

50S

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polysomes are

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When small and large subunits undergo of the ribosome associate with each other and the mRNA, translate the target mRNA, then dissociate after each round of sythesis.

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translation occurs

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substrate(s) for a round of amino acid addition are

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The bond between the aminoacyl-tRNA and the amino acid is not broken during the formation of the next peptide bond.

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What drives the peptide bond formation?

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ribosomal RNAs are represent the main component of the ribosome because

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what are the three binding sites for tRNA on a ribosome

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peptidyl transferase center

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what allows only unpaired RNA to pass through the small and large subunit of the ribosome?

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channel is through the small subunit which is only wide enough to let unpaired mRNA through and too narrow for a structure. Ensures that codons in mRNA will be exposed and available for pairing with the anticodon loops of tRNA.

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the kink in the mRNA between two codons are included after ribosome translocation to not allow any entry of the mRNA

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channel lets nascent polypeptide through. Some secondary structures can form inside but some can't. But and quaternary structure will not be formed until after its exit the ribosome.

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Successful initiation in translation occurs when?

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translation initiation in prokaryotes is mostly done in the absence of the full ribosome

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Specialized charged tRNA that binds directly to the P site and not the A site during initiation.

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One of the three initiation factors, that binds to the small subunit and block its from reassociating with the large subunit or from binding charged tRNAs.

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purple-one of the three initiation factors in prokaryotes, it is a GTAPase which interacts with IF 1, charged initiator tRNA, and the small subunit.
yellow-prevents tRNAs from binding to the portion of the small subunit that will become part of the A site.

IF 1

IF 4

IF 3

IF2

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the last step in initiation is the 70s initiation complex, where fmet-tRNA, start codon, base pair which allows the small subunit to undergo a conformational change.

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In eukaryotic initiation, the 43s pre-initiation complex

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recognition of eukaryotic mRNAs after 43S pre initiation complex,

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once the complex is assembled at the 5' end of the mRNA, they move along the 5'-3' direction by a process that ATP-dependent

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The reason why the initiator tRNA must bind to the small subunit before it binds to the mRNA is because it is used in scanning by recognizing the start codon through base pairing between anticodon of tRNA and start codon.

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The binding of the large subunit to the small subunit in eukaryotes

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Poly-A-binding protein and eIF4G interact by the 5' and 3' end of the mRNA to

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Exceptions to eukaryotic polypeptide being encoded by an open reading frame that starts with AUG?

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eIF4G adaptor role when an mRNA is capped?

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Elongation is very different in prokaryotes and eukaryotes.

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Whats this step in this mechanism?

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When EF-Tu is bound to GDP and lacking any bound nucleotide it shows high affinity for aminoacyl-tRNAs.

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What are one of the three mechanisms that contributes to the fidelity of codon recognition?

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Third mechanism in correct codon-anticodon incorporation is ( accommodation, GTP hydrolysis ), which is rotation of tRNA into the peptidyl transferase center.

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Reason why ribosome is a ribozyme?

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23S rRNA catalyzes peptide bond formation by base pairing with the CCA variable loop of the tRNAs in the A and the P sites with help position alpha amino go of aminoacyl tRNA to attack carbonyl of growing peptide attached to peptidyl-tRNA.

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( EF-G, EF-Tu ) is an elongation factor that completes translocation by binding to the ribosome's factor binding center with GTP.

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( molecular mimicry, all elongation factor ) in which a protein takes on the appearance of a tRNA to facilitate association with the same binding site.

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Exchange of GDP for GTP for both EF-TU-GDP and EF-G-GDP are? ( in order)

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Eukaryotic factors analogous to EF-Tu (( eEF1, EIF1A )) and EF-G(( eEF2, EF-Tu )) are name differently but have similar function.

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how many molecules of ATP and GTP are used for peptide bond formation?

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Termination of translation is done by

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the name of the codon on the release factor the recognizes a stop codon?

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Class II release factor RF3,

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RRF

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Puromycin is an aminoglycoside antibiotic which binds to the 16rRNA causing misreading of the genetic code

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tetracycline is a polyketide, which block the p site.

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puromycin

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SsrA

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What is this mechanism?

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what machanism is this?

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protein mediated regulation in bacteria

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riboswitches are

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regulation of translation by small RNA (sRNA) in bacteria

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initiation in eukaryotic translation is globally regulated by

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gene specific regulation of translation through cap sequestration in eukaryotes

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