unit 11 part 2 Flashcards

(37 cards)

1
Q

rna splicing

A
  • removes introns
  • creates a continuous molecule with readable coding sequence
  • carried out by the spliceosome
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2
Q

Spliceosome

A
  • A variety of proteins and several small RNAs that recognize the splice sites
  • The RNAs of the spliceosome also catalyze the splicing reaction
  • Functions as a ribozyme (RNA enzyme)
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3
Q
  • Ribozymes:
A
  • catalytic rna molecule that functions as enzyme and splice rna
  • not all biological catalysts are proteins
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3
Q
  • Three properties of RNA enable itt o function as an enzyme:
A
  • can form 3d structure becuase of its abilit to base-pair with itself
  • some bases in rna contain functional groups that may participate in catalysis
  • rna may hydrogen bond with other nucleic acid molecules
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3
Q

Some introns contain sequences that

A

mya regualte gene expression

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4
Q

alternative splicing

A
  • Some genes can encode for more than one polypeptide, depending on which exons get included during splicing:
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5
Q

Splicing Results

A
  • Proteins often have a modular architecture consisting of discrete regions called domains
  • In many cases, different exons code for the different domains in a protein
  • Exon shuffling may result in the evolution of new proteins
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6
Q

Understanding Translation

A
  • Genetic information flows from mRNA to protein through the process of translation
  • Translation creates a polypeptide from the mRNA information
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7
Q

transfer RNA (tRNA)

A
  • tRNAs transfer amino acids to the growing polypeptide in a ribosome
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8
Q
  • Each tRNA molecule enables translation of a specific mRNA codon into a certain amino acid
A
  • Each carries a specific amino acid on one end
  • Each has an anticodon on the other end
  • Anticodon base-pairs with a complementary codon on mRNA
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9
Q

3D Structure of tRNA

A
  • Single RNA strand that is~80 nt long
  • Flattened into one plane to reveal tRNA base pairing, looks like a cloverleaf
  • Hydrogen bonding twists tRNA into 3D molecule
  • tRNA is roughly L-shaped with the 5’and3’ ends both located near one end of the structure
  • The protruding 3’ end acts as an attachment site for an amino acid
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10
Q

Ribosomes

A
  • Ribosomes facilitate specific coupling of tRNA anticodons with mRNA codons in protein synthesis
  • The two ribosomal subunits (large and small):
  • Made of proteins and ribosomal RNA (rRNA)
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11
Q

A site

A

holds the tRNA that carriers the next amino acid to be added to the chain

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12
Q

P site

A

holds the tRNA that carriers the growing polypeptide chain

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13
Q

E site

A

is the exit site where discharged tRNA leave the ribosome

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14
Q
  • The three stages of translation:
A
  • Initiation
  • Elongation
  • Termination
  • Energy is required for some steps
15
Q

Synthesizing a polypeptide - Initiation

A
  • The start codon (AUG) signals the start of translation
  • A small ribosomal subunit binds with mRNA and a special initiator tRNA
  • The small subunit moves along the mRNA until it reaches the start codon (Met)
  • Proteins called initiation factors bring in the large subunit that completes the translation initiation complex
16
Q

Synthesizing a polypeptide - Elongation

A
  • During elongation, amino acids are added one by one to the C-terminus of the growing chain
  • Each addition involves proteins called elongation factors
  • Translation proceeds along the mRNA in a 5′ → 3′ direction
  • The ribosome and mRNA move relative to each other, codon by codon
17
Q
  • Elongation occurs in three steps
A

codon recognition, peptide bond formation, and translocation
* Requires energy during the first and third steps

18
Q

Synthesizing a polypeptide - Termination

A
  • Elongation continues until a stop codon in the mRNA reaches the A site of the ribosome
  • The A site accepts a protein called a release factor
19
Q

Release factor

A

causes the addition of a water
molecule instead of an amino acid
* Hydrolysis, splits bond between tRNA and polypeptide
- energy is required

20
Q

translation folding protein does what

A
  • During translation, polypeptide chain spontaneously folds into 3D molecule
  • A gene determines primary structure, and primary structure in turn determines shape
  • Often translation is not sufficient to make a functional protein
21
Q

Post Translational Modifications

A
  • Polypeptide chains are modified after translation or targeted to specific sites in the cell
  • Post-translational modifications may be required before the protein can begin doing its particular job in the cell
  • Examples: protein cleavage, phosphorylation, acetylation
22
Q

Ribosomes
- Ribosomes are identical and can switch from free to bound

A
  • free ribosomes (cytosol)
  • Free ribosomes mostly synthesize proteins that function in the cytosol
  • bound ribosomes (attached to ER)
  • Bound ribosomes make proteins of the endomembrane system and proteins that are secreted from the cell
22
* Polypeptide synthesis always begins in the
cytosol - synthesis finishes in the cytosol unless the polypeptide signals the ribosome to attach to the ER
23
Polypeptides destined for the ER or for secretion are marked by a
signal peptide
24
* A signal-recognition particle (SRP)
Binds to the singal peptide on the N terminus * The SRP escorts the ribosome to a receptor protein built into the ER membrane * Polypeptide synthesis resumes, sending polypeptide into ER lumen
25
* Polyribosome (or polysome):
* Multiple ribosomes can translate a single mRNA simultaneously * Polyribosomes enable a cell to make many copies of a polypeptide very quickly
26
Bacterial Processes
* A bacterial cell ensures a streamlined process by coupling transcription and translation * Occuratsametime * In this case the newly made protein can quickly diffuse to its site of function
27
Mutations
* Mutations are changes in the genetic information of a cell * Mutations of one or a few nucleotides can affect protein structure and function * If a mutation has an adverse effect on the phenotype of the organism * Referred to as a genetic disorder or hereditary disease
28
Spontaneous mutations can occur during errors in
DNA replication, recombination, or repair * Mutagens are physical or chemical agents that can cause mutations
29
* Point mutations:
changes in just one nucleotide pair of a gene * The change of a single nucleotide in a DNA template strand can lead to the production of an abnormal protein * Point mutations within a gene can be divided into two general categories: * Single nucleotide-pair substitutions * Nucleotide-pair insertions or deletions
30
* Point mutations:
changes in just one nucleotide pair of a gene * The change of a single nucleotide in a DNA template strand can lead to the production of an abnormal protein * Point mutations within a gene can be divided into two general categories: * Single nucleotide-pair substitutions * Nucleotide-pair insertions or deletions
31
* Silent mutations:
* No effect on the amino acid produced by a codon because of redundancy in the genetic code * Due to Wobble
32
* Missense mutations:
* Still code for an amino acid, but not the correct amino acid
33
* Nonsense mutations:
* Change an amino acid codon into a stop codon * Most lead to a nonfunctional protein
33
* Insertion or deletion (in/del)
of nucleotides often alters the reading frame, producing a frameshift mutation * Depends if in/del is a multiple of three * These mutations may have a disastrous effect on the resulting protein