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Molecular Diagnostics > Lecture 3: Gene Expression: Translation / Protein Synthesis > Flashcards

Lecture 3: Gene Expression: Translation / Protein Synthesis Flashcards

1
Q

Transcription + Translation =

A

Gene Expression

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2
Q

Section of DNA (a gene) being transcribed & translated to produce a protein.

A

gene expression

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3
Q

Genes can be turned on and off (called ___________) by various mechanisms.

Occur at any point during gene expression, but most commonly occurs at the
level of ___________.

A

gene regulation

transcription

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4
Q

Gene regulation:

Signals from the environment or from other cells activate proteins called
_____________ factors which control the level of transcription.

A

transcription

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5
Q

What are regulatory elements in transcription process?

A

Enhancers and suppressors

-Genes are turned on and off in different patterns during development stages

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6
Q

There are the 20 biologically active amino acids in humans. They are
encoded directly by the codons of the universal genetic code are called
__________ or ____________ amino acids.

A

standard, canonical

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7
Q

There are _____ Essential amino acids (indispensable) amino acid , which
cannot be synthesized de novo ), and have to get them from diet.

A

9

– histidine, isoleucine, leucine, lysine, methionine, phenylalanine, threonine,
tryptophan, and valine.

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8
Q

Basic amino acid structure:

a central alpha carbon covalently bonded to…

A

-a carboxyl group
-an amine group
-a hydrogen
-a variable R group

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9
Q

a sequence of three nucleotides that together form a unit of genetic code in a DNA or RNA molecule, and the genetic information is translated into proteins by living cells.

A

Codon

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10
Q

Amino acids are the structural units (monomers) that make up

A

proteins.

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11
Q

There are the 20 biologically active amino acids in

A

Humans

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12
Q

They are
encoded directly by the codons of the universal genetic code are called

A

standard or canonical amino acids

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13
Q

There are _________ Essential amino acids (indispensable) amino acid , which
cannot be synthesized de novo ), and have to get them from __________

A

There are nine Essential amino acids (indispensable) amino acid , which
cannot be synthesized de novo ), and have to get them from diet

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14
Q

nine essential AA

A

histidine, isoleucine, leucine, lysine, methionine, phenylalanine, threonine,
tryptophan, and valine

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15
Q

Amino Acids join together to form short polymer chains called _____________
or longer chains called either __________ or __________.
*

A

peptides
or longer chains called either polypeptides or proteins.
*

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16
Q

Basic Amino Acid Structure

a central alpha carbon covalently linked to:

A

a central alpha carbon covalently linked to:

  • Carboxyl group
  • an amine group
  • a hydrogen
  • a variable R group
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17
Q

The Genetic Code

Codon

A

– a sequence of three nucleotides that together form a unit of genetic code in a DNA
or RNA molecule, and the genetic information is translated into proteins by living
cells.

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18
Q

The Genetic Code

Nonoverlapping and universal in

A

plant and animal kingdoms (ex. Mitochondrial code)

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19
Q

The Genetic Code

Degenerate (wobble base codon

A

– The first two positions of the mRNA codon observe Watson-Crick base pairing rules
(A-U, C-G) The third position exhibits wobble

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20
Q

The genetic code

codon read by

A

Read by complementary tRNA linked to aa

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21
Q

Initiation codon

A

AUG (met)

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22
Q

Stop codons

A

UAA, UGA, UAG

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23
Q

Translation

Information what

high what

A
  • Information decoding
  • High energy consuming process
    – consumes 90% of cells energy
    – 4 ATP / aa
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24
Q

Protein Synthesis Players

A
  • Ribosome / rough ER / rER (rRNA + protein)
  • tRNA = anticodon with aa
  • mRNA = codon
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25
Protein Synthesis Players Ribosome has 2 sites which associate with mRNA
– P site (initaition) – A site (elongation)
26
Protein Synthesis Steps Initiation
– 1st aa always methionine (Met) at P site – Template = mRNA – mRNA moves down in register (A site) and codon is read by anticodon of tRNA
27
Protein Synthesis Steps Elongation
– new aa brought in to match new codons and peptide bonds formed
28
Protein Synthesis Steps Termination
Stop codon (UGA,UAA,UAG)
29
Massager RNA (mRNA) Carries instructions from DNA to where tells the ribosome what
* Carries instructions from DNA to the rest of the ribosome. * Tells the ribosome what kind of protein to make
30
Transfer RNA (tRNA)
A go-getter. Gets the right parts to make the right protein according to mRNA instructions
31
Ribosomal RNA (rRNA) Part of the _____ helps in ______
* Part of the structure of a ribosome * Helps in protein production
32
Ribosomal RNA (rRNA) Ribosomes contain two ______ and 50 or more ________ rRNA sequences are widely used for ________
* Ribosomes contain two major rRNAs and 50 or more proteins * rRNA sequences are widely used for working out evolutionary relationships among organisms
33
Ribosomal RNA (rRNA) Prokaryotic rRNA
size 70s large subunits- 50s and 23s small subunits: 30s
34
Ribosomal RNA (rRNA) eukaryotic rRNA size
size: 80s large subunits- 60s and 28s small subunit- 40s
35
End Product of protein synthesis
* The end products of protein synthesis is a primary structure of a protein. * A sequence of amino acid bonded together by peptide bonds.
36
Post Translational Modification and Regulation Recognition of
Signal Peptide
37
Post Translational Modification and Regulation Glycosylation O linked N linked
addition of sugars to proteins destined to be membrane or secreted – “O” linked- serine/threonine in golgi – “N” linked - asparagine in ER
38
Post Translational Modification and Regulation Proteolysis cleavage-
Truncation
39
Post Translational Modification and Regulation _______ bonds bridges Attachment or binding of groups _________
Disulfide bonds bridge NAD,Zn,Mg,FAD
40
Post Translational Modification and Regulation Assembly of ______
multiple subunits
41
Post Translational Modification and Regulation ______ group modifications
R
42
R -Group Modifications
* Phosphorylation (via kinase on -OH group of serine/threonine/ tyrosine) * Methylation * Acetylation (palmitylation C16 via thioester with cysteine, myristication C14 at amino-terminal glycine) * Isoprenation (farnesyl,guanosyl groups) * Hydroxylation
43
Phosphorylation via
kinase on -OH group of serine/threonine/ tyrosine)
44
Acetylation
palmitylation C16 via thioester with cysteine, myristication C14 at amino-terminal glycine)
45
Isoprenation
arnesyl,guanosyl groups
46
Maturation of Human Pre-Pro-insulin Pre-pro-protein A protein precursor that contains a ______________
a protein precursor that contains a signal peptide sequence; it is a nonpolar sequence at the head of the growing polypeptide chain and contains many hydrophobic amino acids residues.
47
48
Maturation of Human Pre-Pro-insulin Pre-pro-protein required for its transfer into the ________ of the ______________; the signal sequence is then cleaved to form the protein or proprotein.
required for its transfer into the cistern of the endoplasmic reticulum; the signal sequence is then cleaved to form the protein or proprotein.
49
Insulin Protein Precursors: Pro-Insulin Pre-pro-sequence About ___ non polar aa guide the protien to be
– About 30 non-polar aa guide the protein to be secreted out of cells or into different compartment of the cell sub-organells
50
Insulin Protein Precursors: Pro-Insulin Pro-sequences Areas where Usually in the transition of May be involved In
– areas in the protein that are essential for its correct folding – usually in the transition of a protein from an inactive to an active state. – Pro-sequences may also be involved in pro-protein transport and secretion
51
Clinical Usage of C peptide Measurement * Patients with ________ may have their C-peptide levels measured as a means of distinguishing type ________ from type _________ or __________
* Patients with diabetes may have their C-peptide levels measured as a means of distinguishing type 1 diabetes from type 2 diabetes or Maturity onset diabetes of the young (MODY).
52
Clinical Usage of C peptide Measurement * Measuring __-peptide can help to determine how much of their own natural insulin a person is producing as C-peptide is secreted in ________ amounts to _________.
* Measuring C-peptide can help to determine how much of their own natural insulin a person is producing as C-peptide is secreted in equimolar amounts to insulin.
53
Clinical Usage of C peptide Measurement C-peptide levels are measured instead of _________ because C-peptide can assess a person's own _________ even if they receive _________ injections
C-peptide levels are measured instead of insulin levels because C-peptide can assess a person's own insulin secretion even if they receive insulin injections
54
Clinical Usage of C peptide Measurement * Because the liver does not metabolize ____-peptide, meaning blood C-peptide may be a better measure of ______ _______ secretion than insulin itself.
* Because the liver does not metabolize C-peptide, meaning blood C-peptide may be a better measure of portal insulin secretion than insulin itself.
55
Clinical Usage of C peptide Measurement A very low C-peptide confirms Type ____ diabetes and insulin ___________ and is associated with high glucose variability, hyperglycaemia and increased complications.
A very low C-peptide confirms Type 1 diabetes and insulin dependence and is associated with high glucose variability, hyperglycaemia and increased complications. Hyperglycemia- recent increase in sugar levels not due to a underlying condition
56
Genetic Codon Change Causes Mutation in Proteins Point mutation missense and nonsense mutation
* Point Mutations – No change-silent due to alteration in 3rd base of codon, wobble or degenerate base – Missense- change in base leads to change in aa – Nonsense-formation or modification of termination codon
57
Genetic Codon Change Causes Mutation in Proteins Frameshift mutation
insertion or deletion of a nucleotide
58
Diseases Related to Mutations a-thalassemia (Nonsense) – normally 142 aa long – If stop codon at 142 mutates get a 172 aa version including these variants:
* Constant Spring: glutamine @ 142 * Icaria: lysine @ 142 * Seal Roe: glutamate @ 142 * Koya Dora: serine @ 142
59
* Thalassemia- Frameshift Mutation Abnormal Hemoglobin Wayne
everything after 138 is incorrect (goes to 147 before stop)
60
Inhibitors of Protein Synthesis Streptomycin and erythromycin
Streptomycin / Gentamycin: 30S prok. initiation * Erythromycin: Target 50S prok. Elongation, both Gram + and Gram - bacteria
61
Inhibitors of Protein Synthesis Chloramphenicol and cyclohexamide
* Chloramphenicol: 70S ribosomal subunit in prok, elongation, broad spectrum, bone marrow suppression * Cyclohexamide: 80S euk translocation step, and fungus etc
62
Inhibitors of Protein Synthesis Tetracycline and Puromycin
* Tetracycline: Inhibits incoming tRNA to A site at 30S subunit in prokaryotes * Puromycin: Premature terminator both prok and euk, mimic tRNA binds at A site, resistant to hydrolysis
63
Inhibitors of Protein Synthesis Diphtheria toxin
Euk elongation factor II inhibitor
64
Antibiotics Bind to Ribosome The following antibiotics bind to the 30S subunit of the ribosome:
– Aminoglycosides – Tetracyclines
65
Antibiotics Bind to Ribosome The following antibiotics bind to the 50S ribosomal subunit:
– Chloramphenicol – Erythromycin – Streptogramins- a group of cyclic peptide antibiotics that inhibit, like macrolides and lincosamides, the synthesis of bacterial proteins.
66
Streptogramins
a group of cyclic peptide antibiotics that inhibit, like macrolides and lincosamides, the synthesis of bacterial proteins.
67
Hemaglobulin Constant springs
Mutation at the stop codon at 142aa and gets elongated to a 172aa chain. Glutamine @ 142
68
C peptide can be release in the blood and then
Get measured for a marker for Diabetic patients
69
Pre-pro- insulin sequence Pre sequence
Has a lot of + charges of a single peptide sequence so it can go through the lipid bilayer once it passes the bilayer the Pre sequence is removed
70
Pre-pro- insulin sequence Pro sequence
This is where digestions and endonuclease cleavage happens into active insulin
71
Glycosylations of what molecular is common
Immunoglobulins
72
30s what does the S stand for
Size
73
Nonoverlapping
When mRNA is synthesized, it will read every three nucleotides without jumping
74
How two Aminoacids are linked
Carboxyl chain is linked to the N terminal with the removal of water
75
+ charged Amino acids
Lysine Histidine Arginine
76
Negative Charged Amino acids
Aspartic acid Glutamic acid
77
AZT is used for patients with
AIDS and is where H-N-H binds to promotor regions and inhibits it
78
Rifampin is used to treat
Tuberculosis
79
Prokaryotes have almost no
modifications such as G-cap
80
Alternate splicing is where what is removed
Exons
81
Pre-mRNA is what
Introns and extrons but introns get removed
82
Splicing is
where introns are removed
83
Specific enzymes cut the primary transcript of mRNA, tRNA, and rRNA to make individual RNAs
Endonucleases
84
The promotor sequence is recognized by
RNA polymerase
85
The CAAT, GC, and TATA box are all located where
Upstream and are part of the promotor region and is toward the left side
86
Upstream of RNA
does not directly transcribe RNA but may regulate it
87
RNA is synthesized with only one strand of
DNA
88
Polymerase 3 is the main
Processive enzyme
89
P= Rho factor=
Stops synthesis= Rho dependent
90
SIgma subunit
Recognizes sequence in DNA template= promotor region
91
Cofactors for RNA synthesis
Mg2+, Fe2+, and Zn2+
92
RNA can be self folded into many shapes such as
Hair pin and step loop shaped

Molecular Diagnostics (12 decks)

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