Genetics test 5 Flashcards
functions of protein macro level
form structures - hair, scales, feathers
glow to act as a signal between organisms
Be used to kill - rattlesnake venom
Functions of protiens within and between cells
Machines - DNA polymerase, ATP synthase, Dynein
Signals - Insulin, Oxytocin, Leptin
Structures - microtubules, actin, membrane channels
acidic amino acids
Non essential
negative charge
hydrophilic
ionic and hydrogen bonds
basic amino acid
lysine
positive charge
hydrophilic
ionic and hydrogen bonds
neutral polar amino acids
threonine
no charges
nuetral nonpolar amino acids
tryptophan
phenylalanine
valine
isoleucine
leucine
methionine
hydrophobic
start codon
AUG
Stop codon
UAA
UAG
UGA
amino acids are linked together via
peptide bonds
Protien structure language
a chain of amino acids is a peptide or polypeptide
one oe more chains together may be a protien
protiens have structure: primary, secondary, tertiary, and quartenary
Primary structure of protiens
order of amino acids in polypetide chain
secondary structure of protiens
regular folding of a single chain
maintained by weak bonds (hydrogen pairing)
ALPHA helix or BETA sheet
Tertiary structure of protiens
three-dimensional structure of an entire polypeptide chain
Quartenary structure of protiens
arragement of multiple polypeptides into a single multi-subunit complex
Structure of tRNA
75-90 nt long - different sequences
cloverleaf configuration
loop 2 contains anticodon
each tRNA binds one amino acid
anticodon
tRNA anticodon pairs with its complementary codon on the mRNA molecule
appropriate amino acid is inserted into the polypeptide
charging of tRNA
one ATP required
aminoacyl tRNA synthetase enzyme catalyzes reaction
molecules are chemically linked to proper amino acids
amino acids converted to active form - reacts with ATP to create aminoacyladenylic acid
Bacterial/prokaryotes ribosomes
70S = 50S (large) + 30S (small)
50 has 23S and 5S rRNA
30 has 165 rRNA
unit arranged as 5’–16S–23S–5S–3’
transcibed as single pre-rRNA transcript, but bound by ribosomal protiens and cleaved by enzymes co-transcriptionally to produce ribosomal complex
bacteria only have one RNA polymerase, so it also transcibes this RNA
Eukaryotic ribosomes
80S = 60S (large) + 40S
Large subunits have 28S, 5.8S and 5S rRNA
Small subunits contain 18S rRNA
Unit arranged as 5’–18S–5.8S–28S–3’
pre-rRNA is enzymatically cleaved by RNA pol III, the massive transcription from the tandem copies leads to nucleolus formation
The 5S rRNA is transcribed from a separate locus - RNA Pol I
ribosome site A
aminoacyl site
where the incoming charged tRNA binds
ribosome site P
aminoacyl site
where a tRNA bound to the growing polypeptide chain sits
ribosome site E
exit site
where a free uncharged tRNA preparing to exit the ribosome sits
shine dalgarno
relationship between start AUG and shine-dalgarno sequence
shine dalgarno binds to a complementary sequence in the 16S rRNA
shine-dalgarno sequence is located in the 5’ UTR of mRNA about 8-12 nts before the AUG start codon
prokaryotic initiation of translation
1) load mRNA onto small subunit
2) load first tRNA
3) add large subunit, kick out IF’s, hydrolyze GTP
Step 1 of prokaryotic initation of translation - load mRNA onto small subunit
Initiation factor-1 blocks A site
IF-3 blocks 50S attachment
helps mRNA binding to 30S
shine-delgarno sequence complementary to 16S rRNA in 30S subunit
Step 2 of prokaryotic initation of translation - load first tRNA
since A site is blocked and E site doesn’t exists, tRNA loads into P site
IF-2 brings a special fMET tRNA for iniation in prokaryotes
how are eukaryotic initation of translation different
IF’s = eIF’s and there are many more than 3
Initiator Met is NOT modified
no shine-dalgarno
Best model is scanning model for identifying start
Key points in the scanning model
eIF-4e is “cap binding protien’ (binds 5’ cap on mRNA)
the poly-a-tail loops around and is involved through association with eIF-4F and eIF-4G
the 40S subunit, bound to Met-tRNA
Met loads onto 5’ end and slides along looking for an AUG that is not a Kozak sequence
elongation
Once 70S initiation complex is formed, fMet-tRNA
fMEt is bound to AUG codon in the P site of the ribosome
1) Next charged tRNA loaded into the A site
2) peptide bond formation
3) translocation
4) repeat steps 1-3
elongation step 1
EF-Tu (elongation factor 2) TS and GTP/GDP are required to bring new tRNA’s to the ribosome for elongation
elongation step 2
peptide bond forms between the two adjacent amino acids, catalyzed by peptidyl transferase
The linked amino acids are attached to the tRNA in the A site, forming a peptidyl-tRNA
elongation step 3
the ribosome shifts doen one codon
the empty tRNA is ejected from the E site
the tRNA + growing chain shifts to P site, the A site is empty again
termination
1) stop codon is encountered
2) release factor (RF1) binds to stop codon
3) polypeptide chain is released
4) RF3-GDP binds causing RF1 relase. GTP replaces the GDP and GTP hydrolysis relases RF3
5) ribosome recycling factor (RRF) binds to A site
6) EF-G-GTP binds to ribosome. Hydrolsysis of GTP tp GDP causes translocation of the ribosome, putting RRF in the P site, and the tRNA in the E site
7) RRF relases the uncharged tRNA, EF-G then releases RRF, and the two ribosomal subunits dissociate from the mRNA
tetrapeptide
a polypeptide made up of four or more amino acids
N-terminus
Amino group
C-terminus
Carboxyl group
R-group
will differ based on the amino acid
a-carbon
carbon at the center of the amino acid
peptide bond
bond between amino acids
inducible enzymes
bacteria adapt to environment by producing inducible enzymes only when specific substrates are present
constitutive enzymes
enymes are continuously produced regardless of the chemical makeup of the environment
positive control
transcription occurs only when regulator molecule directly stimulates RNA production
negative control
genetic expression occurs unless shut off by regulator milecule