The sequence of three nucleotides located on the anticodon arm of the tRNA
cloverleaf structure. The anticodon bonds in antiparallel fashion with a codon
of mRNA at the acceptor site of a ribosome during translation.
The smaller of two prokaryotic ribosomal subunits. Responsible for binding to
the ribosome binding site on the mRNA.
The larger of the two prokaryotic ribosomal subunits. Binds after the small
subunit binds to mRNA, creating the initiation complex.
The prokaryotic ribosomal complex formed by the binding of the small and
large subunits. Responsible for carrying out DNA translation on an mRNA strand.
A three-nucleotide position in a ribosome that binds to an aminoacyl
tRNA, a tRNA molecule bearing an amino acid.
One secondary structural feature of tRNA. Contains the sequence CCA and has a
free 3' OH. Binds to the amino acid.
The first step in tRNA charging. Involves the
"activation" of an amino acid
so that the acid can be bound to a tRNA molecule. The process of activation
involves the transfer of an AMP group from ATP to the amino acid.
A tRNA molecule that has been charged. It is loaded with an amino acid and
is ready to participate in translation at the ribosome, where it binds to
the acceptor site.
The enzyme that catalyzes the bond between specific tRNA and amino acid, to form
A secondary structural feature of tRNA. Contains the anticodon that base
pairs with an mRNA codon during translation.
A chemical functional group made up of a carbon double-bonded to an oxygen and
single-bonded to an OH group.
The two-step process in which an amino acid is "loaded" onto a
tRNA. The first
step is adenylylation; the second is the binding of tRNA and amino acid into
an aminoacyl tRNA.
Term used to describe a tRNA molecule that has been loaded with an amino acid
and is ready to participate in translation.
The two-dimensional structure of tRNA, resembling a cloverleaf, and caused by
One of the unusual bases found in tRNA. Contains two additional hydrogens in
place of the double bond that is usually found in uracil.
A secondary structural feature of tRNA. Contains a number of dihydrouridines.
GTP-dependent proteins that help bring aa-tRNA to the acceptor site of a
ribosome during translation. Elongation factors also help in the
translocation process. Energy is supplied by the hydrolysis of GTP to GDP.
Proteins that help associate pieces of the initiation complex.
A carbon-nitrogen chemical bond formed between amino acid subunits of a
A three nucleotide position in a ribosome in which
peptidyl tRNA is
The name given to the tRNA located in the P site of the ribosome during
translation. This tRNA holds the growing polypeptide chain.
The enzyme responsible for catalyzing the peptide bond formation reaction
between amino acids in the P site and A site of a ribosome during
A chain of many peptide, or amino acid, subunits joined together through peptide
Term used to describe a group of separate ribosomes that are bound to the same
One of the unusual bases found in tRNA in which the normal 1' nitrogen site of
ribose attachment is switched to the 5' carbon position.
A protein that recognizes one of three stop codons on an mRNA chain. Its
binding results in the release of the completed polypeptide chain and the
dissociation of the 30S and 50S subunits.
The structure in the cell, made up of protein and RNA (rRNA), that functions as
the "factory" of protein synthesis. Ribosomes contain a binding site for mRNA,
and three binding sites for tRNA: the acceptor site, the peptidyl site,
and the exit site.
Ribosome binding site
An approximately 10 nucleotide sequence found in a prokaryotic mRNA strand that
is recognized and bound by the ribosome. Located 5 to 11 nucleotides from
the initiator codon. In eukaryotes, the ribosome binding site
functionally replaced by the 5' cap.
A secondary structural feature of tRNA. Contains the sequence thymine-
pseudouridine-cytosine in its stem loop.
The process in which the ribosome moves three nucleotides down an mRNA
strand in the 3' direction. Process is catalyzed by the hydrolysis of GTP to