2.16 Protein Processing Flashcards

1
Q

Portions of a nonfunctional protein are removed, resulting to release of an active protein

A

Cleaving

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

Responsible for removing these portions by breaking their peptide bonds

A

Endoproteases

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

Inactive precursors of enzymes

A

Zymogens

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

inactive form of trypsin

A

Trypsinogen

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

Inactive form of chymotrypsin

A

Chymotrysinogen

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

Inactive precursors of hormones

A

Prohormones

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

Covalent attachment of chemical groups to protein

A

Altering

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

Modifications by altering include:

A

Phosphorylation
Glycosylation
Hydroxylation
Other covalent modifications (Carboxylation and Farnesylation)

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

Addition of phosphate groups by kinases

A

Phosphorylation

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

Occurs on hydroxyl groups of serine, threonine and less frequently in tyrosine

A

Phosphorylation

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

Addition of carbohydrate to form glycopreoteins

A

Glycosylation

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
12
Q

Important in producing antigenic properties of proteins

A

Glycosylation

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

Used for protein targeting and signaling

A

Glycosylation

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

Addition of hydroxyl groups by hydroxylases

A

Hydroxylation

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

Glutamate residues are carboxylated to become gamma-carboxyglutamate

A

Carboxylation

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
16
Q

Attachment of lipids for anchoring proteins to membranes

A

Farnesylation

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
17
Q

Proteins that are aberrant are tagged for destruction

A

Degrading

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
18
Q

Located almost everywhere in the cell and tags aberrant proteins

A

Ubiquitin

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
19
Q

Destroys abberant proteins

A

Proteasome

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
20
Q

Enzymes hydroxylates and oxidizes specific AA (proline, lysine)
Amino terminal peptides are cleaved off

A

Procollagen

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
21
Q

Multiple ribosome units are translating the same mRNA

A

Polyribosomes/polysomes

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
22
Q

Polysomes are located in ___ or within ___

A

Cytosol

RER

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
23
Q

Protein sorting occurs via two pathways:

A

Cytosolic pathway

Rough endoplasmic reticulum pathway

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
24
Q

Proteins for the nucleus, peroxisome, mitochondria, cytosol

A

Cytosolic pathway

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
25
Membranes, lysosomic enzymes, secretory proteins
RER pathway
26
Signal sequences produced in initial translation will determine if the protein will be fully synthesized in free cytosol or rough ER
Signal Hypothesis
27
Components of signal hypothesis
``` Signal sequence Signal recognition particle SRP receptor Translocator Signal peptidase ```
28
Ribonucleoprotein that consists of a 7s RNA with 300 nucleotides and 6 different proteins
Signal recognition particle
29
Nuclear localization proteins
Nucleus
30
Peroxisomal-matrix targeting sequences
Peroxisome
31
Targeting proteins to the matrix
Mitochondria
32
RER pathway
Membranes (Plasma, ER, BGA) Lysosomes Secretory proteins
33
Pancreatic cancer cells
Zymogens
34
Pancreatic beta cells
Insulin c-Peptide Amylin
35
Fibroblasts
Collagen Elastin Glycoproteins Proteoglycans
36
Goblet cells
Glycoproteins (mucins) | Proteoglycans
37
Intestinal mucosal cells
Chylomicrons
38
Hepatocytes
Serum albums Other plasma proteins VLDL
39
Type of processing | All proteins of secretory pathway
Removal of signal sequences
40
Type of processing | Most proteins of secretory pathways
Disulfide bond formation
41
Type of processing Collagen Other glycoproteins Proteogrlycans
Glycosylation
42
Type of processing Collagen Elastin
Amino acid modifications
43
Type of processing Insulin Other peptide and protein hormones
Partial proteolytic cleavage
44
Process of ingesting large particles such as viruses, bacteria, cells or debris
Phagocytosis
45
Occurs in specialized cells such as macrophages and granulocytes
Phagocytosis
46
Intake of a protein from outside the cell via a receptor then parts of the plasma membrane form a protective vesicle around it
Phagocytosis
47
Uptake of fluid and fluid content, smaller molecules, primarily inorganic molecules
Pinocytosis
48
Cell drinking
Pinocytosis
49
Nonselective process of solute uptake
Fluid-phase pinocytosis
50
A more specific uptake of macro molecules that utilize membrane-bound receptors
Absorptive pinocytosis
51
Receptor-mediated pinocytosis
Absorptive pinocytosis
52
Two types of pinocytosis
Fluid-phase pinocytosis | Absorptive pinocytosis
53
Proteins will adhere to specific receptors and need to be arranged in a way so that certain vesicle-forming molecules will be able to property form their vesicles around them
Receptor-mediated endocytosis
54
Vesicle-forming molecules
Clathrin-adaptin molecules
55
Functions of receptor-mediated endocytosis
Uptake of substances Waste disposal Mucosal transfer
56
Process wherein the substance is endocytosed in one side of a celll and is exocytosed to the other side
Transcytosis
57
Protein responsible for phagocytosis
Actin
58
Proteins responsible for receptor-mediated endocytosis
Actin Clathrin Adaptin
59
Process where a defective organelle enclosed by formation of a double bilayer vesible around it
Macroautophagy
60
Present in all four endocytic pathways that serve as end points of ingested substances Vesicles acting as recycling centers
Lysosomes
61
Lysosomes contain hydrolytic enzyme usually produced by ____
RER
62
Cells are unable to degrade materials, hence, these are being accumulated in the lysosome
Lysosomal storage diseases
63
Neimann-pick Tay-Sachs Fabry Farber
Lipid-storage diseases
64
Hunter and hurler
Glycoprotein-storage diseases
65
Pompe
Glycogen-storage disease
66
Sequnce of AA | Dictates the final shape/folding of protein
Primary structure
67
alpha-helix | beta-pleated sheets
Secondary structure
68
3-d conformation of a polypeptide
Tertiary structure
69
Interaction of more than one tertiary structure
Quaternary structure
70
Responsible for binding to hydrophobic areas and prevents improper folding Has ATPase acitivity
Chaperone
71
Affected protein | Cystic fibrosis
CFTR
72
Affected protein | Hemophilia A
Factor VIII, IX
73
Affected protein | Von Willebrand disease
von Willebrand factor
74
Affected protein | Tay-sachs disease
B-hexominase
75
Affected protein | Familial hypercholesterolemia
LDL receptor
76
Affected protein | alpha1-antitrypsin deficiency
alpha1-antitrypsin
77
Inactivates eEF-2
Diphtheria toxin
78
Inactivates 28s RNA
Ricin
79
A-site of ribosome: aminonucleoside analogue (fake tRNA forming an amide bond)
Puromocyin
80
30s subunit or small ribosomal subunit (prevents initiation)
Aminoglycosides
81
30s subunit of small ribosomal subunit (prevents binding of aminoacyl tRNAs to A-site)
Tetracycline
82
50s subunit or large ribosomal subunit | Inhibits peptidyltransferase
Chloramphenicol
83
50s subunit or large ribosomal subunit (inhibits translocation)
Clindamycin/erythromycin
84
23s subunit
Macrolides
85
60s subunit
Cycloheximide