4 RNA polymerases RNA processing Splicing of pre-mrna Introns Vs exons tRNA Protein synthesis Post-transitional modifications Chaperone protein Flashcards

1
Q

RNA polymerases have no proofreading function in ____ (prokaryotes/eukaryotes).

A

Eukaryotes

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2
Q

A gardener finds a cap mushroom and decides to eat it. Later, liver failure develops. How did this happen?

A

The mushrooms likely contain α-amanitin, which inhibits RNA polymerase II and causes severe hepatotoxicity

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3
Q

In eukaryotes, ____ makes tRNA, ____ makes mRNA, and ____ makes rRNA
RNA polymerase

A

III; II; I

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4
Q

Of the RNA types, ____ is the largest RNA, ____ is the most abundant RNA, and ____ is the smallest RNA.

A

mRNA; rRNA; tRNA (massive, rampant, and tiny, respectively)

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5
Q

In prokaryotes, which enzyme makes rRNA, mRNA, and tRNA?

A

RNA polymerase (one single multisubunit complex)

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6
Q

Where does RNA polymerase II open DNA?

A

At the promoter site

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7
Q

What is rifampin’s mechanism of action?

A

Inhibition of RNA polymerase in prokaryotes

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8
Q

What is actinomycin D’s mechanism of action?

A

Inhibition of RNA polymerase in both prokaryotes and eukaryotes

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9
Q

Where does eukaryotic RNA processing occur?

A

In the nucleus

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10
Q

Which three modifications take place during eukaryotic RNA processing?

A

Capping on the 5′ end, polyadenylation on the 3′ end, and splicing out of introns

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11
Q

Approximately how many adenosine monophosphates are added to the 3′ end of mRNA during polyadenylation?

A

200

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12
Q

What is the term for the initial (unprocessed) RNA transcript in eukaryotes?

A

Heterogeneous nuclear RNA (hnRNA)

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13
Q

What function does the sequence AAUAAA serve in eukaryotes?

A

Polyadenylation signal

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14
Q

Poly-A polymerase ____ (does/does not) require a template.

A

Does not

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15
Q

A science experiment is done to add the 7-methylguanosine cap. Where does this occur in the cell?

A

In the nucleus—it is added to the 5′ end of the hnRNA

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16
Q

What is the role of cytoplasmic P-bodies in RNA processing?

A

Location of mRNA quality control—accomplished using exonucleases, decapping enzymes, and micro-RNAs

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17
Q

What binds to a primary mRNA transcript and forms a spliceosome?

A

Small nuclear ribonucleoprotein particles (snRNPs) and other proteins

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18
Q

snRNPs form a lariat-shaped loop in order to do what?

A

Isolate an intron for removal

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19
Q

A patient presents with a malar “butterfly” rash and renal disease. What antibodies does her disease make?

A

She has lupus, associated with spliceosomal snRNP antibodies (anti-Smith); mixed connective tissue disease (MCTD) has anti-U1 RNP antibodies

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20
Q

____ (Exons/Introns) contain the genetic information to code for protein.

A

Exons (exons exit and are expressed)

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21
Q

What is the name for the intervening noncoding segments of DNA within a gene?

A

Introns (introns are intervening sequences and stay in the nucleus)

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22
Q

β-thalassemia mutations can result from ____, a process that combines exons to make unique proteins in different tissues.

A

Alternative splicing, which, in this case, yields a pathologic protein

23
Q

What mechanism allows the same gene to encode for multiple proteins?

A

Alternative splicing

24
Q

A patient’s cancer cells undergo genetic analysis. What splicing-related phenomenon may be implicated in the tumor’s initial oncogenesis?

A

Abnormal splicing variants

25
Q

What part of a tRNA lies opposite from its 3′ aminoacyl end?

A

The anticodon end

26
Q

Which three-nucleotide sequence do all eukaryotic and prokaryotic tRNAs have at their 3′-ends?

A

CCA (Can Carry Amino acids)

27
Q

• Where on a tRNA does the amino acid that will be incorporated into the protein bind?

A

The 3′ end

28
Q

Does charging a tRNA molecule with an amino acid require energy?

A

Yes, as ATP is hydrolyzed in the process

29
Q

If a tRNA had a methionine bound to it, what would the sequence of the codon it binds read, in 5′-to-3′ order? And the anticodon?

A

Codon = AUG; anticodon = CAU

30
Q

• What are the substrates of the reaction that is catalyzed by aminoacyl-tRNA synthetase (the “matchmaker”)?

A

The uncharged tRNA and the appropriate amino acid, ATP

31
Q

What does aminoacyl-tRNA synthetase do?

A

It scrutinizes the amino acid before and after it binds to tRNA, hydrolyzing the bond if an incorrect amino acid is present

32
Q

Which sequence is necessary for tRNA-ribosome binding?

A

Thymine, pseudouridine, cytosine (TΨC), found on the T-arm

33
Q

What is the purpose of the D-arm?

A

Ensures identification by the correct aminoacyl-tRNA synthetase

34
Q

What hypothesis states that only the first two positions of a triplet codon on mRNA have a precise pairing with the tRNA anticodon?

A

Wobble hypothesis

35
Q

The wobble hypothesis primarily explains the ____ (unambiguous/degeneracy/universal/commaless) nature of the genetic code.

A

Degeneracy

36
Q

What are the two subunits of the eukaryotic ribosome called?

A

The 60S subunit and the 40S subunit—40S + 60S leads to 80S (Eukaryotic = Even)

37
Q

____ (Eukaryotes/Prokaryotes) have ribosomes with 50S and 30S subunits.

A

Prokaryotes; 30S + 50S leads to 70S (prOkaryotes are Odd)

38
Q

A scientist studying protein synthesis wants to block initiator methionine tRNA. He makes an inhibitor blocking the A site. Will this work?

A

No, as the initiator methionine tRNA does not bind at the A site (it is the sole exception; all other aminoacyl-tRNA combinations bind here)

39
Q

At the start of protein synthesis, what process occurs at the same time as the hydrolysis of methionine’s bond with its tRNA?

A

The formation of a peptide bond between methionine and the second amino acid in the polypeptide

40
Q

When referring the “P site” of a ribosome, what does the “P” stand for?

A

Peptide—the P site accommodates the growing polypeptide chain

41
Q

Which molecules are responsible for assembling the 40S subunit with the initiator tRNA?

A

Eukaryotic initiation factors (IFs)

42
Q

In what direction relative to the mRNA does the ribosome shift after the formation of a peptidyl bond?

A

Toward the 3′ end

43
Q

When the ribosome shifts after the formation of a peptidyl bond, to what position does the tRNA with the growing peptide chain go?

A

The P site (translocation)

44
Q

What molecule provides the energy for the binding of tRNA to the ribosome/mRNA complex?

A

Guanosine triphosphate (GTP tRNA = Gripping)

45
Q

What molecule provides the energy for the translocation of the ribosome along the mRNA?

A

Guanosine triphosphate (GTP tRNA = Going places)

46
Q

When the ribosome shifts after the formation of a peptidyl bond, where is the uncharged tRNA found?

A

• In the E position (holds Empty tRNA as it Exits

47
Q

In protein synthesis, what are the three steps of protein elongation?

A

Aminoacyl-tRNA binding to A site, transfer of growing peptide chain to amino acid at the A site by the ribsome, and, finally, translocation

48
Q

A patient takes an antibiotic that blocks the prokaryotic 30S subunit from assembling. How does it interfere with protein synthesis?

A

It inhibits formation of the initiation complex, causing misreading of mRNA

49
Q

• A patient with a MRSA infection takes an antibiotic that inhibits translocation by binding the 50S subunit. Does this affect human cells?

A

No—the 50S subunit is prokaryotic, so human cells are minimally targeted by this drug

50
Q

In termination, what recognizes the stop codon and frees the completed protein from the ribosome?

A

Release factor

51
Q

What is an example of protein trimming after translation?

A

Removing N- or C-terminal propeptides from a zymogen to yield a mature protein (example: conversion of trypsinogen into trypsin)

52
Q

A scientist wants to write about covalent alterations. Name six kinds of posttranslational protein modifications that are involved.

A

Phosphorylation, glycosylation, hydroxylation, methylation, acetylation, and ubiquitination

53
Q

• What is a chaperone protein?

A

An intracellular protein that is involved in facilitating and/or maintaining protein folding

54
Q

A scientist studies Hsp60, a protein expressed in yeast to prevent misfolding at high temperatures. How are these proteins classified?

A

Heat shock proteins̬class of chaperone proteins that facilitate and maintain proper protein folding)