Translation: Initiatioin

Front 1

binding of ribosome to ___ of mRNA for synthesis from ___ of protein

Back 1

5'-terminus

n-to c-terminus

Front 2

energy input of protein synthesis is__-

Back 2

GTP

Front 3

What does protein synthesis involve?

Back 3

initiation factors, elongation factors and termination factors

Front 4

mRNA being read by ___ ribosomes

Back 4

multiple

Front 5

initiator tRNA

Back 5

charge with N-formyl-methionine (fMet)

Front 6

binding of ribosome to ___ of mRNA for synthesis from ___ of protein

Back 6

5'-terminus

n-to c-terminus

Front 7

energy input of protein synthesis is__-

Back 7

GTP

Front 8

What does protein synthesis involve?

Back 8

initiation factors, elongation factors and termination factors

Front 9

mRNA being read by ___ ribosomes

Back 9

multiple

Front 10

initiator tRNA

Back 10

charge with N-formyl-methionine (fMet)

Front 11

ribosome binds at a conserved 5' ______ 10 bases upstream of AUG.

Back 11

untranslated region (UTR)

Front 12

shine-dalgarno sequence

Back 12

AGGAGGU

Front 13

adaptive immune system

Back 13

immune cells remember previous encounters with pathogens...slow to develop

Front 14

innate immunity

Back 14

not specific to a particular pathogen....recognizes specific features of pathogens by presence of formylmethionine containing peptides (potent chemoattractants for neutrophils)

Front 15

translation initiation complex

Back 15

initiation factors IF1, IF2, IF3

Front 16

IF1 and IF3 keep___

Back 16

30S free

Front 17

IF1

Back 17

blocks A site

Front 18

IF3

Back 18

binding with mRNA

Front 19

IF2

Back 19

joins and fmet tRNA finds

Front 20

only fmet-tRNA enters

Back 20

P site

Front 21

only alpha alpha-tRNA enters

Back 21

A site on complet 70s ribosome

Front 22

EF-Tu

Back 22

elongation bound to GTP...
followed by EF-G bound by GTP

Front 23

Tu-GDP remains bound to allow...

Back 23

dissociation of incorrect tRNA

Front 24

first peptide bone formation by what enzyme?

Back 24

peptidyl transferase activity in 23S rRNA of the large subunit of RNA enzyme

Front 25

GTP binding elongation factor EF-G cause

Back 25

exit of tRNA from P site, movement of peptidyl tRNA to P site and ribosome movement by 3 bases along the mRNA

Front 26

Do tRNAs recognize stop codons?

Back 26

no, they are recognized by relase factors (FR)...to cleave release polypetide from tRNA and mRNA and dissociate of ribosome subunits

Front 27

antibioitc bind selectively to various sites on

Back 27

ribosomes

Front 28

cycloheximide

Back 28

inhibits peptidyl transferase in euk (60S ribosome)

Front 29

chloramphenicol

Back 29

inhibits peptidyl transferase in prok (50S)

Front 30

puromycin

Back 30

causes premature chain termination during protein syntheis...in both eu and pro (50S and 60S)

Front 31

streptomycin

Back 31

inhibits initiation by binding to the 30S ribosomal subunit

Front 32

erythromycin

Back 32

inhibits translocation by binding to 50S ribosome

Front 33

tetracycline

Back 33

binds 30S ribosome and prevents animoacyl-tRNA binding

Front 34

eukaryotes have what for initiation?

Back 34

40S initiation complex
tRNAi with own aminoacyl t-RNA synthetase to form complex

Front 35

eIF2 interacts with

Back 35

only Met-tRNAiMet (not other Met-tRNA

Front 36

eukaryotic mRNAs may be held in a ____ by initation factors

Back 36

circular conformation:
eIF4s and eIF3

Front 37

selection of eukaryotic translation initiation site requires:

Back 37

1. helicase
2. movemtn of complex
3. ATP

Front 38

eIF4s bind to

Back 38

"cap", poly a, mRNA, 40s ribosomal subunit

Front 39

eIF4 helicase activity

Back 39

unwinds the secondary structure of RNA

Front 40

intitation complex migrates from ___ to ___

Back 40

5'-end cap to the first AUG

Front 41

Kozak sequence

Back 41

needs to be found to initiate translation in eukaryotes...5'-CCACCAUGG-3'

trial and error approach

Front 42

Where is the 80S initiation complex formed?

Back 42

at AUG, 60S joins the 40S initiation complex

GTP of eIF5 is hydrolyzed

Front 43

EF1alpha

Back 43

elongation facotr is GTP binding=> peptidyl-transferase makes peptide bond in 28S rRNA

Front 44

does EF1alpha interact with tRNAimet

Back 44

no

Front 45

what is required for translocation?

Back 45

EF2-GTP
uncharged tRNA exits via the E site

Front 46

TPO

Back 46

thrombopoietin:
produced in relatively low amounts in nermal cells
ligand for c-MpI recepter and regulates the production of platelets

Front 47

hereditary thrombocythemia

Back 47

autosomal dominant disorder
high levels of TPO

Front 48

Excess production of TPO is attributed to:

Back 48

mutations in TPO gene that restructure 5' sequence in mRNA...effiecient translation initation at actual AUG start codon

Front 49

Mdm2 protein

Back 49

oncogene that accelerates degradation o f p53, a tumor suppressor protein

Front 50

50% of mutations of what are in tRNA genes?

Back 50

mitochonrial diseases

Front 51

1/3 of inherited huma diseases result form )))

Back 51

premature termination codon mutation (PTC)

Front 52

aminoglycoside antibiotics

Back 52

binding to ribosome rduces fidelity of translation,
a codon can be recognized by pairing with 2-bases of the codon...so the protein should turn out normal

Front 53

ricin

Back 53

eukaryotic ribosome inhibitor protein
bioterriorism by KGB
.enzyme that depurinates a specific "A" residue on 28S rRNA of ribosome

Front 54

protein domains being ___ while the protein is still being synthesized.

Back 54

folding

Front 55

molten globule

Back 55

open flexible protein structure forms right after synthesis...

Front 56

folding into the final tertiary sturcture leads to the formation of ___

Back 56

mature protein

Front 57

What are the two types of proteins required for protein folding?

Back 57

chaperones
cahperonins

Front 58

Hsp70

Back 58

a chaperone class. binds the hydrophobic pathces of protein folds.
ATP hydrolysis facilitates folding the regions back into protein in right conformation

Front 59

chaperonins

Back 59

cylindrical macromolecular assembly that directly facilitates folding

Front 60

a chaperone:

Back 60

binds unfolded or partially folded proteins and prevent their aggregation

Front 61

What happens if the first folding is misfolded?

Back 61

It goes to a protease pathway:
degradee by proteolysis

Front 62

What is the significance of proteolytic fragments ?

Back 62

they can aggregate and cause degenerative diseases

Front 63

Alzheimer's disease

Back 63

amyloid precursor protein (APP) is cleaved into Abeta42 product that accumulates