Glossary of Cell Biology Exam Chapter 7
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- RNA directed protein synthesis
- Eukaryotic mRNA
- single strand of ribonucleotides;
processing occurs in nucleus;
reads in 5' to 3' direction
- Start codon
- AUG (Met)
- Stop codon
- UAA, UGA, UAG
- Eukaryotic tRNA
- single strand of 70-80 ribonucleotides;
adaptor molecule between mRNA and amino acid;
folds into L structure;
has 3' CCA;
- 3' CCA
- site of amino acid attachment
- 3 nucleotide residue sequence;
specifies particular amino acid
- the reduced specificity of hydrogen bonding between the third base on the codon and anticodon
- Anticodon is _______ to codon.
- Eukaryotic ribosome (80S)
- large subunit (60S) consists of 28S, 5.8S, and 5S rRNA;
small subunit (40S) consists of 18S rRNA and 30 proteins
- Eukaryotic rRNA
- 45S pre-rRNA: transcribed in nucleolus;
5.0S rRNA: transcribed outside nucleolus and inside nucleus
- Three stages of Translation
- In what direction do ribosomes move along mRNA?
- 5' to 3'
- In what direction is protein synthesized?
- N terminal to C terminal
- short sequence of RNA complementary to region of specific mRNA; upon binding, the RNAi catalzes the destrucution of the mRNA to which it binds
- What is the destinantion of free ribosomes?
- What is the destination of membrane-bound ribosomes?
- plamsma membrane
- Folding of proteins
- primary amino acid sequence assumes final three dimensional conformation
- Modification of proteins
- covalent bond formation;
addition of constituents such as sugars, lipids, and phosphorlyation
- What is the function of chaperones?
- Chaperons aid in folding.
- What is the function of Hsp70?
- prevents premature folding
- What is the function of Hsp60?
- protects protein from surrounding environment to allow protein to fold slowly
- Name the two enzymes that alter covalent bonds during protein folding.
- PDI-Protein Disulfide Isomerase;
Peptidly Prolyl Isomerase
- Protein Disulfide Isomerase
- insures proper disulfide bond formation between cysteine residues
- Peptidly Prolyl Isomerase
- catalzyes isomerization of peptide bonds involving proline
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