translation Flashcards
(29 cards)
what is translation?
RNA -> protein, translating message into a final product: protein or polypeptide chain
what is the difference between polypeptide chain and protein?
some proteins are comprised of more than one polypeptide chain
what does the end product of translation represent?
the nucleotide sequence present in the gene of interest
what is special about the DNA sequence?
they occur in triplets that yield complementary triplets of nucleotides in the mRNA
what are each of the nucleotide triplets in mRNA known as?
codons
what is the genetic code?
all of the codons and the amino acids they code for
what are the two regions of tRNA that are special?
- anticodon that binds to a specific codon in mRNA
- carries amino acid that corresponds to the codon
how does tRNA appear in the cell with its specific amino acid attached?
tRNA ligase: by a family of 20 tRNA synthetase enzymes
true or false: each tRNA synthetase enzyme recognizes one and only one amino acid and attaches it to its appropriate tRNA
true
what happens when the enzyme has bound both serine and its tRNA?
charging/loading tRNA: the enzyme then uses the energy in ATP to create a bond between serine and the tRNA
what is the purpose of rRNA?
combines with other proteins to form a ribosome
what is the purpose of the ribosome?
provides the scaffolding needed to combine the appropriate amino acids in the right sequence to form the protein being synthesized.
what are the two subunits of the ribosome?
50S and 30S
what is the key step in the translation process of eukaryotic cells that involve 30S subunit, mRNA and a specific initiator tRNA carrying methionine?
the 30 S subunit moves along the mRNA until it locates and binds to the ‘start codon’, AUG. At this point, the two subunits come together creating a passageway through which the mRNA that is to be translated moves.
what is the combination of the two ribosomal subunits, the strand of mRNA, and the initiator tRNA comprise known as?
the ‘translation initiation complex’
describe the passageway of the ribosome through which tRNAs move and their anticodons bind to the codons on the mRNA via A,E, and P site
the first tRNA that helped initiate the process, has already bound to the start codon on the mRNA. This tRNA sits in what is known as the ‘P site’ within this passageway. Based on the second codon, the tRNA with the appropriate anticodon and amino acid enters the passageway. This tRNA then binds to the mRNA in the region of the ribosome called the ‘A site’ When this happens, an enzymatic component of the ribosome links the methionine on the first tRNA to the amino acid carried in by the second tRNA. This occurs at the region of the ribosome called the ‘P site’ and the two amino acids are linked with a peptide bond. Once this happens, the ribosome shifts over one codon to allow the first tRNA to leave through the ‘ E site ’. This allows the next tRNA to bind to its codon in the A site, and the process is repeated to elongate the polypeptide one amino acid at a time. In essence, each tRNA with the appropriate anticodon carrying the appropriate amino acid enters, binds, adds its amino acid to the polypeptide and then leaves.
what are the three stop codons?
UAA, UAG and UGA
true or false: tRNA recognizes the stop codons
false
how does the process stop?
release factor enters A site, then an enzymatic reaction occurs that separates the tRNA in the P site from the polypeptide chain. As a result, synthesis of the polypeptide is terminated and it is released through an opening in the 50S subunit.
also causes the 50S and 30S subunits to separate from the mRNA and from each other
what causes a primary protein structure to change shape?
hydrogen bonds form between the amino acids
a hydrogen bond might form between the carbonyl group of one amino acid and the amino group of another one several amino acids down the chain, what could result if it happens several times along the length of the protein? what about hydrogen bonds between other amino acids in the chain
alpha helix
secondary structure: beta sheet, bend or other shapes
what bonds affect tertiary structure?
covalent and non-covalent interactions
what interactions account for the 3D shape of proteins?
- hydrophobic portions of nonpolar amino acids orient themselves so they can avoid the aqueous environment of the cell.
- two sulfur containing amino acids (methionine, cysteine, homocysteine and taurine) in different parts of the protein might form di-sulfide bonds with each other
- positively and negatively charged side groups of amino acids could form ionic bonds.
what is the quaternary structure?
several highly folded proteins are assembled together as subunits that carry out complex functions