Protein Pathway Supplement (2) Flashcards

1
Q

Three stop codons

A

UAA
UAG
UGA

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
2
Q

How many codons code for the 20 known amino acids

A

61

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
3
Q

What is on the 5’ cap of mRNA

What is on the 3’ tail of mRNA

A
A 7-methylguanosine 
A Poly(A) tail
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
4
Q

What is the general structure of tRNA

A

A cloverleaf with two distinct regions of unpaired nucleotides

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
5
Q

Anticodon loop

A

A set of three consecutive nucleotides that paid with a complementary codon in mRNA

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
6
Q

What is an aminoacyl tRNA

A

A complex of tRNA with amino acid

The AA needs to be activated by aminoacyl tRNA synthetases

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
7
Q

Two step process for activation of amino acids

A
  1. Aminoacyl tRNA synthase catalyzes AMP to COOH end of AA

2. AA transferred to cognate tRNA

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
8
Q

Why is it relevant that the structures of prokaryotic ribosomes and eukaryotic ribosomes are different

A

We can target prokaryotic ones with antibiotics

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
9
Q

Describe the A site, P site, and E site

A

Where mRNA codon is exposed to receive aminoacyl tRNA

Where aminoacyl tRNA is attached

Location occupied by empty tRNA before exiting ribosome

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
10
Q

What direction does translation occur

A

5 - 3

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
11
Q

Three steps of translation

A
  1. Initiation - formation of mRNA, small ribosomal subunit and initiator tRNA pre-initiation complex
  2. Elongation - activated AA attached to initiating Met by forming a peptide bond
  3. Termination - peptide chain is release from ribosomal complex
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
12
Q

Translation begins with what

A

AUG (methionine)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
13
Q

What in eukaryotes determines the reading frame for the whole sequence

A

5’, 3’ poly(A), kozak sequence, and the ATP dependent mRNA scan

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
14
Q

The activated AA is attached to initiating methionine how

A

Via a peptide bond

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
15
Q

What three steps involve elongating the peptide chain

A
  1. Loading of an amionacyl tRNA onto the ribosome
  2. Prior to loading, aminoacyl tRNA is attached to a GTP bound elongation factor
  3. Loading is accompanied by GTP hydrolysis
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
16
Q

What enzyme catalyzes the formation of the peptide bond between AA in A and P sites

A

Peptidyl transferase

17
Q

How do RF’s work

A

Bind to A site and cleave the ester bond between C terminus of the polypeptide and the tRNA

18
Q

Describe the cytoplasmic pathway

A

Used for proteins destined for cytosol, mitochondria, mucleus, and peroxisomes

Protein synthesis begins and ends on free ribosomes in cytoplasm

19
Q

Describe the secretory pathway

A

Used by proteins destined for the ER, lysosomes, plasma membranes, or for secretion

Translation begins on free ribosomes but terminates on ribosomes sent to ER

20
Q

Proteins synthesized in cytoplasmic pathway have no what

A

No translocation signals

21
Q

Translocation sequences are recognized by what

A

Transporter in inner membrane (TIM)

Transporter in outer membrane (TOM)

22
Q

What is the signal sequence for ER Lumen proteins

A

KDEL

Lysine, aspartic acid, glutamic acid, leucine

23
Q

What is the signal for lysosomal proteins

A

Mannose-6-phsophate

24
Q

What is the signal for membrane proteins

A

N-terminal apolar regions

25
What is the signal for secretory proteins
Tryptophan domain
26
Glycoproteins can be either what or what
O or N O-Link - formed with the hydroxyl bond of Ser of Thr N-Link - always with Asparagine
27
Describe phosphorylation
Formaiton of an ester bond between phosphate and OH of amino acid through serine/threonine and tyrosine kinase The phosphate is removed by phosphatases Regulates enzyme activity and protein function
28
How does glycosylation attach to a protein
O - linked - through an OH group | N - linked - through a CONH2 group (amide)
29
How does phosphorylation attach to a protein
Through the formation of an ester bond between phosphate and the OH of the amino acid
30
How do disulfide bonds attach to proteins
Through the formation of a thiol (SH) group of two cystine residues
31
How does acetylation attach to proteins
Through Acetyl CoA The histones are acetylated and deacetylated on their N-terminus Lysines
32
Silent mutation
No change to the amino acid
33
Missense mutation
Changes an amino acid within the protein
34
Frameshift mutation
One or more nucleotides are deleted or inserted which causes a change in the codon sequence and alteration in the amino acid