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changes the AA
makes protein bigger |
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Can fuck with DNA POL DNA POL get confused and replicates a region again
mutated seq with too many repeats |
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CAG reapeated
incurable neurodegenerative genetic disorder that affects muscle coordination and some cognitive functions, typically becoming noticeable in middle age. |
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di or trinucleotide repeats |
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usually nonsensical
Ex. cystic fibrosis which lose phe which is stuck in golgi and cannot be processed |
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mrna
fmet tRNA
ribosomal subunits
IF: 1,2,3 promote binding of mRNA to 30s
IF2 hydrolyzes GTP to GDP
After GTP is cleaved 50s subunit binds and IF fall off |
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seq 8-10 bp upstream of AUG. seq base pairing is reqd for AUG to be positioned over shine delgarno |
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binds to AUG through the P site of initiation complex.
Req's gtp binding |
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What is location of tRNA synthesis? |
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nucleolus and via RNA POL I
it made via a 45 S precursor which is cleaved into the mature version |
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Binds to the 30 S subunit which changes the shape of the ribosome. this causes misreading of mRNA--> wrong aa being |
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eIF4 binds 5' cap.
POlyA binding proteins bind to eIF4 and cap complex= activators.
Small subunit is attracted to cap binding proteins--> it attaches along with eIF2, GTP, tRNA complex with met attached. Small subunit scans until it reaches AUG--> triggers the hydolysis of gto via eIF2--> release of ifs and binding of the large ribosomal subunit and translation begins. |
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PP elongates through a tunnel in large subunit. the mRNA is moved not the protein. eEF1 guides a new aa tRNA to the A site.
Gtp hydolysis allows eEF1 to dissociate from tRNA |
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removes highly conserve A from 28s rRNA--> stops translation
removal of one base can inactivate entire 60s subunit (LARGE). |
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Why is Adenine crucial ribosome |
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It is important for the interaction of eEF1 and 2 with the ribosome large subunit. |
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disrupts codon-anti codon interaction by binding the small subunit. this prevents AA tRNA from binding the A site |
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guides new AA tRNA into a site. when gtp is hydolyzed it falls off. if incorrect tRNA is @ A site, it wont hydrolyze gtp |
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the AA attached to tRNA in p site is transferred to tRNA in A site. This is catalyzed by peptidyle transferase (function of large subunit 28s) or 60s. Adenine in active site catalyzes peptide bond via acid base catalysis |
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importance of Adenine to ribosome |
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Definition
very important to 60s subunit. sits in active site for catalysis of peptide bond formation btwn AA in a and p sites. as well as for interaction of ribosome and eEF1 and 2. |
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fuck with the large subunit 23s in prok. affects peptidyl trasnferase activity or formation of peptide bond |
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has the same effect as chloramphenicol but on eukaryotes large subunit 28s. affects peptidly transferase aka peptide bond formation |
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structural resemblence to AA tRNA. incorporated into pp and casuses early termination. affects both euk and prok. |
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advancement of tRNA 3 BP. what was in the P site now moves to e. what was in A goes to P. and A is now empty.
eEF2( EF-G in Prok) drives transloaction via gtp hydrolysis. |
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guides new AA tRNA into A site reqs hydrolysis of gtp
prok analog = EF-TU, EF-Ts
GTP hydrolysis is reqd for it to dissociate |
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drives translocation of ribosome via gtp hydolysis.
prok = EF-G |
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inhibits translation by binding irreversibly to 50s of bacteria, prevents moviemtn |
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same as clindamycin
binds irreversible to the 50s and inhibits translation via preventing movement of ribosome. |
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inhibits eEF2 responsible for trasnlocation. does so by adp-ribosylation |
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recognizes the stop codon in the A site--> hydrolyzes peptidly tRNA bond--> relase of new peptide chain from complex. uses gtp to break up entire complex
EUK RELEASE FACTOR |
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1) translational intiation
2) charging of tRNA
3) attachment of tRNA to a site
4) translocation
5) dissolution of complex. |
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binds 5' cap of mRNA=CBP
attracts small subunit to eventually bind
EUK |
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part of the complex with tRNA, small ribosomal subunit, met.
when it hydrolyzes gtp it causes the release of other intiation factors and is a SIGNAL for Large subunit binding.
ALSO BRINGS first tRNA into P SITE
must have bound gtp |
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iron storage protein.
cell will make more of this when [Fe] is high |
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Plasma membrane receptor which allows for Fe entry into cytosol. production of this protein increase when [Fe] is low. |
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Effects on Ferretin and transferrin synthesis when low [Fe] |
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Ferretin is down regulated by aconitase binding 5' of translational start site
Transferrin is upregulated by aconitase binding to area near 3' stop seq, preventing RNASe from stopping translation |
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Effects of ferretin and transferrin when [Fe] is high |
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Definition
Fe binds aconitase and prevents it from binding 5' of tx start site
aconitase can no longer cover the stop seq for transferring so it will not be expressed as much. |
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