Lecture 4 Flashcards

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1
Q

What is transcription?

A

When we take the information encoded in gene in DNA and encode that information in mRNA.

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2
Q

How is the transcription in prokaryotic cells?

A

Starting with the DNA, from that you code the mRNA.
Then that mRNA can be involved with the ribosome, that that’s the Translation! So no processing happens after RNA polymerase does its job.

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3
Q

Where does the transcription happens in eukaryotic cells (structure)? How many steps (from what to what)?

A

Inside the nucleus.
Two steps:
From DNA -> to pre-mRNA
pre-mRNA -> to mRNA

which can then leave the nucleus and be translated into protein.

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4
Q

The primary actor in the transcription process starts with?

A

The RNA polymerase.

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5
Q

What does the RNA polymerase do?

A

It creates a sequence that will become a nucleotide sequence, then it will become the mRNA.

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6
Q

Where does RNA polymerase starts the process?

A

It attaches to a sequence of the DNA known as promoter.
Then it separates the strands.
After it can code for RNA.

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7
Q

How can the RNA polymerase function when separating the strands? (Hint. DNA replication)

A

Only to 5’ to 3’ direction by adding more nucleotides.

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8
Q

Template strand? Coding strand? Which one does RNA polymerase binds?

A

RNA polymerase binds to the template strand creating same pair as with the coding strand.

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9
Q

Where does the RNA polymerase stops?

A

'’Terminator’’ creates signals to the RNA polymerase that it’s time to stop.

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10
Q

So, the RNA polymerase has stopped its process and formed into ‘‘pre-mRNA’’. What happens next? (Only in eukaryotic cells)

A

At the start:
A 5’ cap, which is a modified guanine, which helps in the translation process.
At the end:
A 3’ end has a poly A-tail.

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11
Q

How does the pre-mRNA splicing happens?

A

Introns are spliced out, because they do not code for the protein.

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12
Q

So basically how does the pre-mRNA proccessing happens?

A

You add the 5’ cap, you add the 3’ end poly A-tail and exons between them.

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13
Q

How do you go from a gene to a protein?

A

From gene to mRNA. (transcription)

From mRNA to Protein. (Translation)

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14
Q

Where does the translation to a protein happen?

A

In a ribosome, where it will be translated into a polypeptide sequence.

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15
Q

What is ribosome made of?

A

Made up of proteins + ribosomal RNA (rRNA)

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16
Q

What does the ribosome do to the mRNA?

A

It travels along the mRNA, from the 5’ end to the 3’ end, reading it, and taking that information, turning it into a sequence of amino acids.

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17
Q

How does the reading of mRNA in ribosome happens?

A

Each of the three nucleotides, a codon (example AUG), the information is encoded in the nitrogenous bases.

18
Q

How do we get from a codon to a specific amino acid? Amount of amino acids?

A

There are 22 standard amino acids, 21, found in eukaryotic cells. 64 permutations, so more than enough for coding for the amino acids.
61 codes for amino acids, 3 STOPS the process.

19
Q

How does the amino acids bind together to form a polypeptide? How do they get matched with a right codon?

A

With transfer RNA (tRNA).
Each of the tRNA’s combine to a specific amino acid.
And with their anti-codons, the pair with the right codon.

20
Q

How does the proper codon - tRNA combination chain actually forms?

A

With three steps:

From left to right:
E-site, P-site, A-site.

21
Q

What is the A-site?

A

A-site is where the appropriate tRNA initially bounds to an amino acid.

22
Q

What happens when the bound of a amino acid happens in the A-site?

A

You have a peptide bond form between the two amino acids, and the ribosome can move to the right. So the A-site goes to the P-site.

23
Q

What are P- and E-sites?

A

P-site is where the polypeptide chain is actually formed.

E-site is ready to exit from the ribosome.

24
Q

How does antibiotics work?

A

In prokaryotic cells in ribosomes we can find molecules that hurt the function of ribosomes.
The antibiotics can interrupt the translation process in the bacteria but not in the cells you want to keep.

25
Q

What is a protein function? (Derived from?)

A

Protein function is derived from three-dimensional structure.
Three-dimensional structure is specified by amino acid sequence.

26
Q

What are proteins structures?

A

Primary, secondary and tertiary structures.

27
Q

Something about primary protein structure?

A

The amino acids linked by peptide bonds into linear chain, based on mRNA sequence.

28
Q

Something about secondary protein structure?

A

Various arrangements resulting from the folding of localized parts of a polypeptide chain.
Structure is stabilized by hydrogen bonds.

29
Q

Something about tertiary protein structure?

A

The overall conformation of a polypeptide chain.

The three-dimensional arrangement of all its amino acid residues.

30
Q

Protein structure is stabilized by?

A

Hydrophobic interactions between the nonpolar side chains.
Hydrogen bonds between polar side chains.
Peptide bonds.

These stabilizing forces hold together elements of secondary structure.

31
Q

How does the folding of proteins happen?

A

It is mediated by proteins - chaparones.

Chaparones bind to the amino (M) terminus of the growing polypeptide chain, stabilizing it in an unfolded configuration until synthesis of the polypeptide is completed.

32
Q

What happens after the synthesis of the polypeptides is completed?

A

The complete protein is then released from the ribosome and is able to fold into its correct three-dimensional conformation.

33
Q

What are isomerases functions?

A
  • Catalyse protein folding
  • Catalyse the isomerization of peptide bonds between proline residues
  • Stabilizes folded structures in many proteins
34
Q

What is proteolysis?

A

Cleavage of the polypeptide chain.

Proteolytic modification play role in the translocation of many proteins across membranes.

35
Q

What is glycosylation?

A

A process where proteins are modified by the addition of sugar.
Glycosylation is initiated in the endoplasmic reticulum before translation is complete.

36
Q

Some proteins are modified in the eukaryotic cells by?

A

Attachment of lipids to the polypeptide chain.

37
Q

Alpha1-antitrypsin deficiency leads to?

A

Lung and liver damage.
Changed forms of this protein fail to complete proper folding and are retained in the ER.
It accumulates in the ER of hepatocytes – the site of synthesis
– resulting in liver damage

38
Q

How does Huntington’s disease forms?

A

Caused by an unstable expansion of a CAG repeats within the coding region of the HTT gene and results in an elongated stretch of glutamine near the N- terminus of the protein.

39
Q

Genes in DNA are expressed when

A

They are read and transcribed into RNA, which is translated into protein by structures called ribosomes.

40
Q

What proteins do?

A

Determines cell’s characteristics and functions.