trancription Flashcards

(60 cards)

1
Q

is the copying of one strand of DNA into RNA by a
process similar to that of DNA replication.

A

Transcription

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2
Q
  • enzyme that catalyzes the process
A

RNA Polymerase

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3
Q

single type of RNA polymerase catalyzes the synthesis of all
RNA.

A

Prokaryotes

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4
Q

binds the RNA polymerase to the
promoter region enabling it to transcribe the DNA

A

sigma subunit-

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5
Q

eukaryotes
RNA Polymerase I
RNA Polymerase II
RNA Polymerase III

A

RNA Polymerase I - synthesis of rRNA
RNA Polymerase II- synthesis of mRNA, snRNA
RNA Polymerase III- synthesis of tRNA, snRNA

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6
Q

needed by RNA polymerase to
bind to the promoter allowing RNA polymerase to bind to the
DNA and read it

A

General Transcription Factor-

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7
Q

location of ribosomal RNA synthesis.

A

Nucleolus

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8
Q

RNA polymerase binds to a specific region of DNA called
the promoter.

A

Initiation

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9
Q

contain specific sequences that help recruit
RNA polymerase and determine which strand of DNA is
transcribed

A

Promoters

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10
Q

Prokaryotic cells

A

-35 region
-10 region (Pribnow box)
+ 1 region

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11
Q

Eukaryotic cells

A

TATA
CAAT
GC

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12
Q

precess wherein RNA polymerases read the template strand

A

Elongation

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13
Q

inhibit RNA polymerase in Eukaryotes

A

Amanitin

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14
Q

inhibit RNA polymerase in Prokaryotes

A

Rifampicin

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15
Q

Once RNA polymerase is bound to the promoter

A

Opens the DNA
Stabilizes the ssDNA
Unwinds the DNA double helix
begins reading the DNA from 3’ to 5’
synthesizing mRNA in the 5’ to 3’ direction.

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16
Q

Transcription continues until RNA polymerase encounters a
termination signal in the DNA sequence.

A

Termination

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17
Q

cause RNA polymerase to detach from the
DNA template, releasing the newly synthesized RNA molecule.

A

Termination signals

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18
Q

causes the RNA polymerase to
break away from the DNA

A

Rho-dependent protein

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19
Q

Hit the areas of inverted repeats creating hairpin loop that
will trigger cleavage enzymes and cleave away from the
RNA polymerase

A

Rho-independent termination

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20
Q

activates particular enzymes and cleaves the RNA polymerase
from the DNA

A

polyadenylation signal (AAUAAA)/ PolyA Site

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21
Q

POSTTRASCRIPTIONAL MODIFICATION OF MRNA

A

1.Capping
2.Polyadenylation
3.Splicing
4. RNA editing

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22
Q

A modified nucleotide, usually 7-methylguanosine, is added to the 5’ end
of the mRNA molecule.

A

Capping

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23
Q

protects the mRNA from exonuclease degradation and helps in
the initiation of translation.C

A

CAP

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24
Q

A polyadenine (poly-A) tail is added to the 3’ end of the mRNA molecule.

A

Polyadenylation

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25
stabilizes the mRNA and is important for mRNA export from the nucleus and translation efficiency.
poly-A tail
26
Many pre-mRNA molecules contain ___________, non-coding regions that must be removed to produce mature mRNA.
introns
27
________ is the process by which introns are removed and ________ (coding regions) are joined together to form a continuous mRNA molecule
SPLICING EXON
28
In some cases, the sequence of the mRNA molecule is altered after transcription by processes such as deamination or nucleotide insertion or deletion.
RNA editing
29
DNA sequences which increases the transcription rate
Enhancers
30
- binds to the enhancer and causes a looping to the DNA
Specific Transcription Factor
31
DNA sequences which decreases the transcription rate
Silencers
32
transcription is controlled by seven major strategies: a
alternative σ factors, RNA polymerase switching, antitermination, enhancers, operon, transcription attenuation, and riboswitch
33
involve the change of transcription machiner
Alternative σ factors, RNA polymerase switching, and antitermination
34
involve the regulation of groups of functionally related genes.
Operon, transcription attenuation and riboswitch
35
are the DNA elements that bind protein factors.
Enhancers
36
GENERAL STRUCTURE OF AMINO ACIDS
amino group carboxyl group α-carbon hydrogen R group
37
determines the identity of the particular amino acid.
R group
38
important for the processes that drive protein chains to fold to form their natural and/or functional structures.
Nonpolar Amino Acids
39
The R group of polar uncharged amino acids can form hydrogen bonds with water and play a variety of nucleophilic role in enzyme reactions
Polar Amino Acid
40
They have carboxyl groups in their side chains in addition to the one present in all amino acids.
Acidic Amino Acids
41
These negatively charged amino acids bind metal ions for structural or functional purposes
Acidic Amino Acids
42
These have a positively charged side chain at physiological pH
Basic Amino Acids
43
The crucial feature of amino acids that allows them to polymerize to form peptides and proteins is the existence of their two chemical groups
amino (-NH+3) carboxyl (-COO-) groups.
44
The peptide bond is an amide bond formed in a____________ between the -COO– group of one amino acid and the-NH+3 group of another amin
The peptide bond is an amide bond formed in a head-to-tail fashion between the -COO– group of one amino acid and the-NH+3 group of another amin
45
AMINO ACIDS CAN JOIN THROUGH PEPTIDE BONDS TO FORM POLYMERS causing q
This reaction eliminates a water molecule and forms a covalent amide linkage.
46
polymers consisting of amino acids linked by covalent peptide bond
Proteins
47
Four levels of protein structure
1. Primary structure The linear sequence of amino acids in a protein chain. 2. Secondary structure The local folding patterns within a protein chain, often forming alpha helices or beta sheets stabilized by hydrogen bonds. 3. Tertiary structure The overall three-dimensional shape of a protein, determined by interactions between amino acid side chains, including hydrogen bonds, disulfide bonds, hydrophobic interactions, and electrostatic interactions. 4. Quaternary structure The arrangement of multiple protein subunits (polypeptide chains) and any associated non-protein molecules into a functional protein complex. Not all proteins have quaternary structure; it only applies to proteins with multiple subunits.
48
3 CLASSES OF PROTEINS BASED ON STRUCTURE AND SOLUBILITY
1.Fibrous Proteins 2. Globular Proteins 3. Membrane Proteins
49
These proteins have elongated, fibrous structures and are typically insoluble in water.
1.Fibrous Proteins
50
These proteins have compact, spherical shapes and are usually soluble in water.
2. Globular Proteins
51
proteins that perform a wide range of functions within the cell, including enzymatic catalysis, transport, and regulation.
2. Globular Proteins
52
proteins that provide structural support and strength to cells and tissues.
1.Fibrous Proteins
53
These proteins are associated with cell membranes and play crucial roles in cell signaling, transport of molecules across membranes, and cell-cell recognition.
3. Membrane Proteins
54
They can have various structures, including integral membrane proteins that span the lipid bilayer and peripheral membrane proteins that are attached to the membrane surface
3. Membrane Proteins
55
is composed of ribonucleotide triplets, known as codons, which specify amino acids.
The genetic code
56
Each codon consists of three ribonucleotide bases and corresponds to a specific amino acid.
Bases: A, G, C, U
57
THE GENETIC CODE how many codnonds
61 codons- code for amino acids 3 codons- stop codons
58
wobble effect refers to a phenomenon in the genetic code where the third nucleotide position of a codon can exhibit flexibility or “wobble” in base pairing during translation.
wobble effect
59
is possible due to the degeneracy of the genetic code, where multiple codons can code for the same amino acid.
wobble effect
60