- Messenger RNA (mRNA), genes that encode proteins.
- Ribosomal RNA (rRNA), form the core of ribosomes.
- Transfer RNA (tRNA), adaptors that link amino acids to mRNA during translation.
- Small regulatory RNA, also called non-coding RNA.
Ribosome is cell organell that consist of 65% RNA – ribosome (RNA-r) and 35% protein ribosome or ribonukleoprotein (RNP) that stick or not on the external surface from RE membrane. Ribosome consist of two sub unit, there are large sub-unit and small sub-unit.
Anatomy of ribosome
- P hole is space to tRNA peptidil.
- A hole is space to amino-asil.
- E hole is exit space to tRNA that will leave from ribosome.
- Ribosome participated bind tRNA and mRNA in located new amino acid at tip of carboxyl.
Biology 8th ed by Campbell and Reece
|
Role of ribosome
- Play important role in protein synthesis as a catalyst.
- The small subunit of ribosome binds mRNA and tRNA
- The large subunits of ribosome play a role in the process of polypeptide bond formation.
http://classconnection.s3.amazonaws.com/768/flashcards/1177768/png/rrna1333777455147.png
|
c. Mechanism of Translation
Video Of Translation Process
- Initiation
Brings together mRNA, a tRNA with the first amino acid, and the two ribosomal subunits.
- First, a small ribosomal subunit binds with mRNA and a special initiator tRNA, which carries methionine and attaches to the start codon.
- Initiation factors bring in the large subunit such that the initiator tRNA occupies the P site.
- Elongation
Consists of a series of three-step cycles as each amino acid is added to the proceeding one, binding of aminoacyl-trna to the a site, peptide bond formation, and translocation.
- Termination
Occurs
when one of the three stop codons reaches the A site.
- A release factor (eRF= RF1). RF1 is bound by a complex consisting of releasing factor RF3 with bound GTP. This complex, with the peptidyl transferase, promotes hydrolysis of the bond between the peptide and the tRNA occupying the P site.
- This frees the polypeptide and the translation complex disassembles.
No comments:
Post a Comment