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Genetic Memory G: Escherichia Cob, 1
Genetic Memory G: Escherichia Cob, 1
Attiarrl
Genetic Memory
G
20014.
JAMA, Nov 25. 1968
. Vol 206,
No 9
Memory-Nirenberg
1973
Table
uuu
l.-The
Genetic
ucu
Code
UAU
PHE
UGU
TYR
CYS
uuc
ucc
UUA
UCA
UAA
TERM
UGA
TERM
UUG
UCG
UAG
TERM
UGG
TRP
cuu
ecu
CAU
UAC
UGC
SER
LEU
CGU
HIS
cut
ccc
LEU
CAC
CGC
CGA
PRO
ARG
CUA
CCA
CAA
CUG
CCG
CAG
ACU
AAU
ACC
AAC
GLN
AUU
CGG
AGU
ASN
AUC
ILE
SER
AGC
THR
ACA
AUA
AAA
AGA
LYS
MET,
is illustrated
in
AUG
MET
GUU
Nov 25,
1968
. Vol 206,
AAG
GCU
GAU
ARG
AGG
GGU
ASP
GUC
1974
ACG
No 9
GCC
VAL
GAC
GGC
GGA
ALA
GLY
GUA
GCA
GAA
GUG
GCG
GAG
GLU
MET,
GGG
Nucleotide
sequences
of RNA codons
were
determined
by stimuWin
binding
of E coli AA-tRNA
to E co/i ribosomes
with trinucleotide
temp T ates.
F-Met
corresponds
to N-formyl-Met-tRNA.
the
initiator
of
protein
synthesis.
TERM
corresponds
to terminator
codons.
u = c
A = G
U = C = A
Genetic
Memory-Nirenberg
Codon Position-Each
triplet can occur in three
structural forms: as a 5-terminal-,
3-terminal-,
or
internal-codon.
Substituents attached to terminal or
internal ribose hydroxyl
groups can influence the
template properties of codons profoundly. Relative
template activities of oligo U preparations, at limiting oligonucleotide
concentrations,
are as follows:
p-5-UpUpU
> UpUpU > CH,O-p4UpUp
>
UpUpU-3-p
> UpUpU-3-p-OCHa
> UpUpU-2,
-3-cyclic phosphate. Trimers with (2-5) phosphodiester
linkages,
(2-5) -UpUpU
and
(2-5) ApApA, do not serve as templates for phenylalanine- or lysine-tRNA,
respectively.
The relative
template efficiencies of oligo A preparations are as
follows: p-5-ApApA
> ApApA > ApApA-3-p
> ApApA-2-p.
Many enzymes have been described that catalyze
the transfer of molecules to or from terminal hydroxyl groups of nucleic acids. It is possible therefore that modifications
of terminal hydroxyl groups
sometimes regulate the reading of RNA or DNA.
Initiation.-Two
species of methionine-tRNA
are
found in E coli; one species, Met-tRNA,
is converted enzymatically
to N-formyl-Met-tRNAi,
and
functions as an initiator of protein synthesis in extracts of E coli in response to the codons AUG or
GUG; the other species, Met-tRNA,,,,
does not accept formyl groups and responds only to AUG.,
Translation
of mRNA is initiated
near the 5terminus of the RNA and proceeds three bases at
a time toward the 3-terminus. The first amino acid
to be incorporated
into protein is the N-terminal
amino acid; the C-terminal amino acid is the last to
be incorporated.
At least three nondialyzable factors are required
for the initiation
of protein synthesis.223 However
the reactions have not been clarified fully. It seems
JAMA,
. Vol 206,
No 9
of Codon Recognition
Memory-Nirenberg
1975
Table 2.-Alternate
Base Pairing
tRNA
Anticodon
u
mRNA
Codon
i2
G
6
I
E
A
Alternate
base
pairing.
The base
in a tRNA
anticodon
shown
an the
left-hand
column
forms
antiparallel
hydrogen
bonds
with
the
base(s)
shown
in the
right
hand
column,
which
:~sually
occupy
the
third
position
of
alternate
mRNA
codobnosnd~elationships
are
wobble
hydrogen
suggested
by
Crlck.30
nize 1, 2 or 3 synonym
codons that differ only in the base
occupying
the third position
of
the codon. Five unique patterns
of degeneracy were found, each
pat tern determined
by alternate
third bases of synonym
triplets
recognized by a tRNA
species.
Patterns of alternate third bases
of synonym codon sets are as follows:
(1) G
(2)
(3)
(4)
(5)
u
A
U
A
=
=
=
=
c
G
C = A
G = U
JAMA,
. Vol 206,
No 9
of translation
can be altered in vivo and in vitro
by altering components or conditions
required for
protein synthesis. The extent of such alterations was
examined by studying the fine structure of the code
with tRNA from different organisms. Almost identical translations
of nucleotide
sequences of amino
acids were found with bacterial,
amphibian,
and
E coli
mammalian
aminoacyl-tRNA.
However,
tRNA did not respond detectably to certain codons.
Therefore aminoacyl-tRNA
preparations
were fractionated by column chromatography
and responses
of tRNA
fractions
to trinucleotide
codons were
determined.
A summary
of the results is shown
in Fig 2.
Many
universal
species of aminoacyl-tRNA
were found, however seven species of mammalian
tRNA were not detected with E coli preparations;
conversely, five species of tRNA from E coli were
not found with mammalian
preparations.
The results also suggest that some organisms contain little
or no aminoacyl-tRNA
for certain codons (AUA,
AGA, or AGG).
The remarkable
similarity
in codon base sequences recognized by bacterial,
amphibian,
and
mammalian
AA-tRNA
suggests that most, perhaps
all, forms of life on this planet use essentially
the
same genetic language. The code probably evolved
more than 5 x 10 years ago.
It is possible that some species-dependent
differences in the codon recognition apparatus serve as
regulators of protein synthesis. The possibility
that
embryonic
differentiation
may be dependent upon
changes in codon recognition
remains to be explored. At the present time, the biological
conseGenetic
Memory-Nirenberg
References
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Vol 206,
No 9
Amino
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-
---~<.
Genetic
II
Memory-Nirenberg
1977