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At least 217 records · Page 12Linked to original sources
PubMed1998

Amino acid contribution to the genetic code structure: end-atom chemical rules of doublet composition.

Up-to-date knowledge is not yet enough to prove or reject completely one of the leading alternative hypotheses considering external or internal origin of the genetic code organization (term "internal" means a peculiarity of amino acids and nucleotides which can propose some logical basis for explanation why definite codons are assigned to particular and not to other amino acids; term "external" in this context implies tRNAs and aminoacyl-tRNA synthetases which provide accuracy of translation but are not presented in the code table in the evident from). New data in favour of the internal approach have been proposed. A close correlation exists between chemical nature of single, the most remote from C alpha, end atoms of amino acid side chains and types of bases in appropriate codon doublets. There are two main rules reflecting this correspondence: (1) all O- or N-ended amino acids (i.e. with O, OO, N, NN, ON, OC and NC end patterns) possess the A-containing codon doublets; (2) all solely C-ended (excluding Ala) and S-ended amino acids (i.e. residues with C, CC and S ends) have the U-containing codon doublets. The discovered asymmetry is characterized by the following high reliable differences of A and U distribution among 21 patterns of individual doublets belonging to 18 amino acids (Pro and Gly are discarded): (a) proportion of A plus U bases corresponding to the two rules, 22/26 is much more than proportion of such bases in violating cases, 4/26; (b) A and U are dominant bases over each of other base types in the doublets of O/N- and C/S-ending amino acids, respectively; (c) the numbers of doublets bearing (18) and not bearing (3) dominant A or U bases are also significantly different. The concept of indicative amino acid end atoms (O/N and non-O/non-N) and doublet A/U bases has been proposed and discussed as so far unknown regulative system of submolecular level of heredity which, additionally to possible key role in the process of the genetic code arising, provides now control of its universality, stability and fidelity.

Amino Acids↗
PubMed1997

Vestiges of early molecular processes leading to the genetic code.

We compare predictions from a proposed model for the origin of the genetic code (J. Theor. Biol (1993) 164, 291-305) with existing information on the base content of codons and abundance of amino acid in different organisms. A comparison is also made between the three groups of amino acids suggested by the model and the two classes of aminoacetyl-tRNA synthetases. The observed agreements tend to support the model.

Amino Acids↗
PubMed1994

On the syntactic structure and redundancy distribution of the genetic code.

By means of an algorithm for finding rules in data, it is shown that the genetic code may be written as a codon-tree, independent of amino acid assignments. Considering this tree as a structural description, a low-complexity, context-free grammar of the code is built and its grammar complexity and grammar redundancy calculated. The relationship between the codon-tree and the hierarchy of amino acid categorizations previously introduced by the author is investigated. Interpreting the obtained code's structure as a record of its evolution, some inferences about the divergences of the code series are made.

Algorithms↗
PubMed1996

The puzzling origin of the genetic code.

Recent results add to the mystery of the origin of the genetic code. In spite of early doubts, RNA can discriminate between hydrophobic amino acids under certain contexts. Moreover, codon reassignment, which has taken place in several organisms and mitochondria, is not a random process. Finally, phylogenies of some aminoacyl-tRNA synthetases suggest that the entire code was not completely assigned at the time of the divergence of bacteria from nucleated cells.

Amino Acids↗
PubMed1995

The phylogeny of tRNAs seems to confirm the predictions of the coevolution theory of the origin of the genetic code.

An extensive analysis of the evolutionary relationships existing between transfer RNAs, performed using parsimony algorithms, is presented. After building up an estimate of the tRNA ancestral sequences, these sequences are then compared using certain methods. The results seem to suggest that the coevolution hypothesis (Wong, J.T., 1975, Proc. Natl. Acad. Sci. USA 72, 1909-1912) that sees the genetic code as a map of the biosynthetic relationships between amino acids is further supported by these results, as compared to the hypotheses that see the physicochemical properties of amino acids as the main adaptative theme that led to the structuring of the genetic code.

Amino Acid Sequence↗
PubMed1995

A deviation from the universal genetic code in Candida maltosa and consequences for heterologous expression of cytochromes P450 52A4 and 52A5 in Saccharomyces cerevisiae.

We demonstrate that serine instead of leucine is specified by the CUG codon in the yeast Candida maltosa. Evidence for this deviation from the universal genetic code was obtained by means of in vitro translation experiments. Depending on the cell-free system used, either serine, in the C. maltosa system, or leucine, in the control with the conventional wheat germ system, was found to be incorporated into the translation products of artificial CUG-containing mRNAs. Moreover, we were able to transfer the non-universal decoding of CUG to the wheat germ system by adding a tRNA fraction isolated from C. maltosa. This finding indicates the presence in C. maltosa of an unusual serine tRNA that recognizes CUG. As a consequence of the altered genetic code, expression in Saccharomyces cerevisiae of C. maltosa cytochrome P450 genes required an exchange of their CTG triplets by TCT encoding serine in order to produce the authentic proteins. In contrast, heterologous expression of the original C. maltosa genes resulted in the formation of still active but unstable enzymes probably subject to selective proteolysis in the host cells.

Base Sequence↗
PubMed2026

Robust error-minimization in the genetic code across physicochemical metrics and variant codes: A graph-theoretic analysis in GF(2)6.

The standard genetic code reduces the impact of point mutations, but the robustness of this property across physicochemical metrics, naturally occurring variant codes, and codon-reassignment mechanisms remains incompletely quantified. Embedding the 64 codons in GF(2)6 represents the hypercube Q6 as a coordinate-dependent subgraph of the encoding-independent single-nucleotide mutation graph H(3,4), and enables continuous &#x3c1;-interpolation between the two. Under a quartet-pattern shuffle null (n=10,000), the standard code is significantly low-cost across four established, code-independent physicochemical distance metrics with partially overlapping content (Grant ham p=0.0062; Miyata p<0.001; Woese polar requirement p=0.003; Kyte-Doolittle hydropathy p=0.001), and the signal strengthens monotonically as &#x3c1; moves Q6&#x2192;H(3,4). A structure-aware sensitivity analysis under the alignment-derived ProtSub matrix (Jia & Jernigan 2021) yields the most extreme percentile of any measure tested (p=0.0004; all five p-values pass Bonferroni at &#x3b1;=0.05). Across the 27 NCBI translation tables, near-optimality is preserved: 11 of 12 informative-distance variants retain top-5% placement after BH-FDR correction. Natural codon reassignments avoid disrupting codon-family connectivity: under the encoding-independent H(3,4) adjacency, observed events are topology-breaking at relative risk 0.32 versus the candidate landscape (permutation p&#x2264;10-4). The H(3,4) result is stable by construction; the Q6 decomposition is representation-specific and fails to show depletion under 8 of 24 base-to-bit encodings, so we report H(3,4) as the primary test and Q6 as a sensitivity. Event-level conditional-logit modelling shows that topology avoidance and local physicochemical cost provide complementary, only weakly correlated signal (rs=0.15), and that topology adds explanatory value beyond physicochemistry under both Q6 and encoding-independent H(3,4) adjacency. Retrospective reanalysis of nine genome-recoding datasets is consistent with codon-family topology operating as an evolutionary-trajectory constraint distinct from acute engineering fitness. The contribution is the second axis: code evolution is jointly constrained by physicochemical smoothness and codon-family topological integrity, and these two constraints are partly independent.

Codon reassignment↗
PubMed1980

The genetic code in bovine mitochondria: sequence of genes for the cytochrome oxidase subunit II and two tRNAs.

Bovine-heart mitochondrial DNA from a single animal was isolated and fragments representative of the entire genome cloned into multicopy plasmid vectors to facilitate determination of its complete nucleotide sequence. We present here the sequence of the region covering the gene for cytochrome oxidase subunit II. Comparison of this sequence with the amino acid sequence of the homologous beef-heart protein has enabled the determination of most of the bovine mitochondrial genetic code. The code differs from the "universal" genetic code in that UGA codes for tryptophan and not termination, and AUA codes for methionine and not isoleucine. The only codon family not represented is the AGA/AGG pair normally used for arginine; evidence from other genes suggests that these code for termination in bovine mitochondria. The sequence presented also includes the adjacent tRNAAsp and tRNALys genes. The tRNAAsp gene is separated by one nucleotide from the 5' end of the COII gene and only three bases separate the 3' end of this gene and the adjacent tRNALys gene. This highly compact gene organisation is very similar to that found in the corresponding region of the human mitochondrial genome and the gene arrangement is identical. The structure of the respective bovine and human tRNAs vary primarily the "D-" and "T psi C-loops".

Animals↗
PubMed1991

Rook's tour representation of the genetic code.

Disconnected recurrences of the stop signal, serine and arginine appear in the original representation of the genetic code, and of the stop signal, arginine, serine and leucine in the codon ring representation. To achieve connectedness along with structural continuity, a rook's tour representation is presented here. On the basis of structural similarities and disparities in their side groups, each of the 20 amino acids is associated with a domain comprised of from one to six contiguous squares on the chess board. As the rook moves on the chess board, it reaches all 64 squares in the ordering of the codon numbers, which prescribe the codons by a simple formula based on the position and size of the nucleotides in a triplet. Recurrences of the stop signal, arginine and serine occur naturally on the tour as the rook enters each of the latter domains for the second time. A mathematical equivalent of the rook's tour may enter as a programming device in the implementation of the code by the RNAs.

Amino Acids↗
PubMed1988

Transfer RNA genes and the genetic code in Chlamydomonas reinhardtii mitochondria.

Only three tRNA genes are present within a sequenced 12.35 kbp region of the 15.8 kbp mtDNA of Chlamydomonas reinhardtii, a unicellular green alga. The corresponding tRNAs, whose anticodons are specific for TGG (Trp), CAA/G (Gln) and ATG (Met) codons, all display conventional secondary structures. The tRNA(Met) gene encodes an elongator rather than initiator species. The standard genetic code is used in C. reinhardtii mitochondria, but codon distribution is highly biased: in a collection of six identified protein coding genes, nine codons (including TGA) are not used at all, while four other sense codons occur very infrequently. In spite of the absence of certain codons, a minimum of 23 tRNAs (assuming separate initiator and elongator tRNAs(Met) are used) is needed to translate the C. reinhardtii mitochondrial genetic code. It appears unlikely that this minimal tRNA set is encoded by C. reinhardtii mtDNA.

Base Sequence↗
PubMed1990

A generalized information function applied to the genetic code.

The problem of the partitioning of the degeneracy of the codons in the genetic code is considered in the framework of a generalized information function IG = c sigma kpk(ln pk + G(Ek] where k represents the number of codons in a specific degeneracy class and G(Ek) is an arbitrary real valued function. For G(Ek) = 0 the Shannon information function is recovered. For a particular choice of G(Ek) that takes the dominance of even degeneracies into account, it is found by direct numerical calculations that the correct degeneracy partitioning appears as optimal values of the Ig function. This results is also supported by optimization calculations in which the generalized information function is regarded as a continuous function in the degeneracy variables.

Amino Acids↗
PubMed1992

Ribosome-mediated incorporation of a non-standard amino acid into a peptide through expansion of the genetic code.

One serious limitation facing protein engineers is the availability of only 20 'proteinogenic' amino acids encoded by natural messenger RNA. The lack of structural diversity among these amino acids restricts the mechanistic and structural issues that can be addressed by site-directed mutagenesis. Here we describe a new technology for incorporating non-standard amino acids into polypeptides by ribosome-based translation. In this technology, the genetic code is expanded through the creation of a 65th codon-anticodon pair from unnatural nucleoside bases having non-standard hydrogen-bonding patterns. This new codon-anticodon pair efficiently supports translation in vitro to yield peptides containing a non-standard amino acid. The versatility of the ribosome as a synthetic tool offers new possibilities for protein engineering, and compares favourably with another recently described approach in which the genetic code is simply rearranged to recruit stop codons to play a coding role.

Amino Acid Sequence↗
PubMed1976

The evolution of a universal genetic code.

Some of the basic problems presented by the rapid evolution of a universal genetic code can be resolved by a mechanism of co-evolution of the code and the amino acids it serves.

Amino Acids↗
PubMed2002

Genetic "code": representations and dynamical models of genetic components and networks.

Dynamical modeling of biological systems is becoming increasingly widespread as people attempt to grasp biological phenomena in their full complexity and make sense of an accelerating stream of experimental data. We review a number of recent modeling studies that focus on systems specifically involving gene expression and regulation. These systems include bacterial metabolic operons and phase-variable piliation, bacteriophages T7 and lambda, and interacting networks of eukaryotic developmental genes. A wide range of conceptual and mathematical representations of genetic components and phenomena appears in these works. We discuss these representations in depth and give an overview of the tools currently available for creating and exploring dynamical models. We argue that for modeling to realize its full potential as a mainstream biological research technique the tools must become more general and flexible, and formal, standardized representations of biological knowledge and data must be developed.

Animals↗
PubMed2002

Expanding the genetic code.

The ability to incorporate unnatural amino acids into proteins directly in living cells will provide new tools to study protein and cellular function, and may generate proteins or even organisms with enhanced properties. Due to the limited promiscuity of some synthetases, natural amino acids can be substituted with close analogs at multiple sites using auxotrophic strains. Alternatively, this can be achieved by deactivating the editing function of some synthetases. The addition of new amino acids to the genetic code, however, requires additional components of the protein biosynthetic machinery including a novel tRNA-codon pair, an aminoacyl-tRNA synthetase, and an amino acid. This new set of components functions orthogonally to the counterparts of the common 20 amino acids, i.e., the orthogonal synthetase (and only this synthetase) aminoacylates the orthogonal tRNA (and only this tRNA) with the unnatural amino acid only, and the resulting acylated tRNA inserts the unnatural amino acid only in response to the unique codon. Using this strategy, the genetic code of Escherichia coli has been expanded to incorporate unnatural amino acids with a fidelity rivaling that of natural amino acids. This methodology is being applied to other cell types and unnatural analogs with a variety of functionalities.

Bacterial Proteins↗
PubMed1996

A non-canonical genetic code in an early diverging eukaryotic lineage.

The nearly invariant nature of the 'Universal Genetic Code' attests to its early establishment in evolution and to the difficulty of altering it now, since so many molecules are required for, and depend upon, faithful translation. Nevertheless, variations on the universal code are known in a handful of genomes. We have found one such variant in diplomonads, an early-diverging eukaryotic lineage. Genes for alpha-tubulin, beta-tubulin and elongation factor 1 alpha (EF-1alpha) from two unclassified strains of Hexamitidae were found to contain TAA and TAG (TAR) triplets at positions suggesting a variant code in which TAR codes for glutamine. We found confirmation of this hypothesis by identifying genes encoding glutamine-tRNAs with CUA and UUA anticodons. The alpha-tubulin and EF-1alpha genes from two other diplomonads, Spironucleus muris and Hexamita inflata, were also sequenced and shown to contain no such non-canonical codons. However, tRNA genes with the anticodons UUA and CUA were found in H.inflata, suggesting that this diplomonad also uses these codons, albeit infrequently. The high GC content of these genomes and the presence of two isoaccepting tRNAs compound the difficulty of understanding how this variant code arose by strictly neutral means.

Amino Acid Sequence↗