Quiz
Regulatory Modifications
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Questions in this quiz (55)
1Regulatory modifications can be removed
- ATrue
- BFalse
2What is added in Palmitoylation?
- APalmitic Acid
- BPalmitoyl-5-Phosphate
- CPalmitite
3The substrate in palmitoylation is added through a thio-ester bond
- ATrue
- BFalse
4Where is the substrate in palmitoylation added?
- AThe central cystine
- BThe two flanking leucines
- COf C/LCL/C
5Describe Model 1 of regulatory modification
- AThe modification changes the functional state (Active --> Inactive or vice versa)
- BThe modification changes the affinity of the protein for its binding partner
6In Model 2, what does the addition do?
- AActivates/deactivates the protein
- BCreates a new binding site that only exists with the modification
- CMarks the protein for destruction
7Phosphorylation is the least used modification in eukaryotic cells
- ATrue
- BFalse
8What is the donor for phosphorylation?
- AGamma phosphate of ATP
- BAlpha phosphate of ATP
- CBeta phosphate of ATP
9Name the two enzymes that add/remove the phosphate
- AProtein kinases
- BProtein phosphatases
- CProtein isomerases
- DProtein transferases
10Phosphates are added to amino acids with OH groups on the R chain
- ATrue
- BFalse
11Phosphorylation can be used for both Model 1 & 2
- ATrue
- BFalse
12Give an example of a Model 1 phosphorylation
- APhosphorylation of Erk Kinase
- BPhosphorylation of tyrosine kinase
- CPhosporylation of Ras
13Describe a Model 2 pathway for phosphorylation
- APlatelet derived growth factor self phosphorylates on Tyr
- BAllows binding of other proteins SH2 domains
- CPhosphorylation of Raf
- DPhosphorylation of MEK
14Acetylation is used almost exclusively for model 1
- ATrue
- BFalse
15To which residue is the substrate for Acetylation added?
- ALysine
- BLeucine
- CTyrosine
16Acetylysine is neutral
- ATrue
- BFalse
17Acetyl-lysines are recognised by what?
- ABromo-domains
- BPhosphoserine domains
- CKH4 domains
18The donor for Acetylation is?
- AN-acetyl glucosamine
- BN-acetyl galactosamine
- CAcetyl CoA
19Name the proteins that add/remove the substrate in acetylation
- AAcetyl Transferase
- BDeacetylases
- CAcetyl Isomerase
- DAcetylase
20How is acetylation used for DNA density regulation?
- AThe histone monomers (H3 & H4 especially) have tails rich in lysine for acetylation
- BT/A residues are acetylated, which signals to move them to the histone and be silenced
- CGTG repeats are acetylated to activate them, moving them away from the histone
21Acetylation causes the DNA to relax
- ATrue
- BFalse
22What is the role of bromodomains?
- ATo interact with histones
- BTo interact with nucleosoems
- CBring in other proteins for the chromatin remodelling complex
23What is the donor substrate for methylation?
- AS-adenosyl Methionine
- BEthanol
- CN-acetyl methionine
24Name the two protein sets that add/remove methyl groups
- AMethyl transferase
- BDemethylase
- CMethyl isomerase
- DMethylases
25There are separate enzymes for lysine and arginine methylation
- ATrue
- BFalse
26Methyl can be added to the same lysine how many times?
- A3
- B4
- C5
27MeK, Me2K and Me3K are all created and recognised by the same enzyme
- ATrue
- BFalse
28Some enzymes can mono/bi/ and tri methylate, some can only do one
- ATrue
- BFalse
29Name the forms of dimethylated arginine
- AMe2R
- BSymmetrical Me2R
- CAsymmetrical Me2R
30What's the difference between s & aMe2R
- AOne is in Cis, the other is in trans formation
- BaMe2R has both methylations on the same arginine
- CaMe2R has both methylations on different arginines
31Arginine has 5 nitrogens to be replaced
- ATrue
- BFalse
32Tudor domains recognise methylation
- ATrue
- BFalse
33Why is S-adenosyl methionine used as the donor
- AIt has a 5-bonded carbon, which makes the methyl easy to remove
- BIt has a 4-bonded phosphate, which makes the methyl easy to remove
- CIt has a 3-bonded sulphur, which makes the methyl easy to remove
34Tandem tudor cannot bind to Me3K as there is no longer a H for it to bind with
- ATrue
- BFalse
35A type of tudor domain will recognise asymmetical Me2R
- ATrue
- BFalse
36ADP ribosylation is mostly Model 2
- ATrue
- BFalse
37What is the donor for ADP ribosylation?
- ANAD+
- BFAD+
- CNADH
38How is the ADP gained from the substrate?
- ACut off the nicotinamide and you're left with the ADP
- BCut off the flavin and you're left with the ADP
39Name the proteins that add/removed ADP
- APoly-ADP Ribose Polymerase
- BADP Transferase
- CDe-ADPase
- DPoly-ADP Ribose Glycohydrolases
40Which amino acids are the ADP(s) added to?
- ALysine
- BGlutamine
- CValine
- DGlutaminc Acid
41Which amino acid has the ADP(s) added?
- ALysine
- BGlutamine
- CValine
42ADP ribose can be addded to ADP ribose in straight or branched chains
- ATrue
- BFalse
43What is the role of glutamic acid ADP ribosylation?
- AHappens to linker histones
- BHappens to open stretches of DNA
- CRecognised by DNA damage response proteins
- DRecognised by silencing proteins
44Name the 3 enzymes used in the addition of Ubiquitin
- AE1- Ubiquitin Conjugating Enzyme
- BE1- Ubiquitin Activating Enzyme
- CE2- Ubiquitin Conjugating Enzyme
- DU2- Ubiquitin Ligase
- EU3- Ubiquitin Activating Enzyme
- FU3- Ubiquitin Ligase
45De-Ubiquitinating Enzyme removes Ubiquitin
- ATrue
- BFalse
46What type of bond forms between Ubiquitin and the target residue?
- AThio-ester, between the COOH of the ubiquitin and the lysine on the target protein
- BIsopeptide, between the COOH of the ubiquitin and the lysine on the target protein
- CDisulphide, between the COOH of the ubiquitin and the lysine on the target protein
47Ubiquitinated lysine 63 are open and flexible and acts a signalling site for complex formation
Ubiquitinated lysine 48 are compact and mark the protein for destruction- ATrue
- BFalse
48What is the first step of ubiquitination?
- AUbiquitin is activated by ATP hydrolysis
- BUbiquitin is activated by GTP hydrolysis
- CUbiquitin is activated by UTP hydrolysis
49Once Ub has been activated, what enzyme does it bind to, and what bond forms?
- AThio-ester
- BPeptide
- CE1
- DE2
50The Ub is then passed on to..
- AE1
- BE2
- CE3
51What is the role of E3?
- ABinding of an E2-Ub complex
- BBinding on an E1-Ub complex
- CBinds to substrate protein & transfers ubiquitin to amino group of lysine
52Protein specificity for Ubiquitination lives in E2
- ATrue
- BFalse
53How many versions of E1 are there?
- A1
- B2
- C3
54There are 35 versions of E2
- ATrue
- BFalse
55How many E3's are there?
- A1
- B10's
- C100's
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- Structural Basis for Biological Function (Protein Modifications) Quiz on Regulatory Modifications, created by gina_evans0312 on 22/12/2013.
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- gina_evans0312
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- English
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