The Evolution of an Enzyme

Bonner, David M.; DeMoss, John A.; Mills, Stanley E.

doi:10.1016/b978-1-4832-2734-4.50028-0

Cited by 45 publications

(22 citation statements)

References 17 publications

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“…The tryptophan synthetases of Neurospora crassa and yeast also provide interesting examples of gene fusion in that they each appear to contain a single polypeptide chain which possesses both types of activities found in the separable A and B chains of E. coli tryptophan synthetase (20). With the immunoglobulins, the internal sequence homology is convincing enough in the constant regions of heavy chains to infer that these regions of the immunoglobulins arose by gene duplication and fusion but that subsequent amino-acid substitutions in the constant regions permitted different functions to be assumed by each constant-region domain (17).…”

Section: Resultsmentioning

confidence: 99%

“…Evidence for complete or partial gene duplication followed by gene fusion has been inferred from studies of proteins such as immunoglobulins (17), phosphofructokinase (18), haptoglobin (19), tryptophan synthetase (20), and ferredoxin (21).…”

Section: Resultsmentioning

confidence: 99%

“…5 was obtained. (15)(16)(17)(18)(19)(20) j&g) was applied to a silica-gel plate, subjected to electrophoresis at pH 6.5, and then chromatographed in pyridine-butanolacetic acid-water. lysine-containing peptides of modified leucyl-tRNA synthetase after digestion with trypsin and S. aureus acid protease.…”

Section: Resultsmentioning

confidence: 99%

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Peptide Mapping of Aminoacyl-tRNA Synthetases: Evidence for Internal Sequence Homology in Escherichia coli Leucyl-tRNA Synthetase

Waterson

Konigsberg

1974

Proc. Natl. Acad. Sci. U.S.A.

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Most aminoacyl-tRNA synthetases contain polypeptide chains of about either 50,000 or 100,000 daltons. Peptide mapping of tryptic, chymotryptic, or Staphylococcus aureus acid protease digests of seryl-tRNA synthetase (100,000, dimer) and leucyl-tRNA synthetase (100,000, monomer) from E. coli was done after selective modification of lysine residues with [ 14 C]succinic anhydride or of methionine residues with [ 14 C]iodoacetate. By use of thin-layer electrophoresis and chromatography on silicagel or cellulose plates followed by radioautography it was possible, depending upon the specific activity of the reagent used, to detect radioactive peptides obtained from as little as l μg of protein. Seryl-tRNA synthetase gave the correct number of tryptic peptides expected for a dimer of identical subunits. Leucyl-tRNA synthetase, on the other hand, gave roughly half the number of radioactive tryptic, chymotryptic, and acid protease peptides expected from the lysine, arginine, and methionine content of the 100,000 monomer. We have interpreted these results as indicating that extensive internal homology exists among lysine- and methionine-containing peptides within the leucyl-tRNA synthetase. The simplest conclusion that can be drawn from these observations is that the NH 2 - and COOH-terminal halves of leucyl-tRNA synthetase and perhaps other synthetases of 100,000 molecular weight may have evolved through a process of gene duplication and fusion, followed by limited diversification by way of amino-acid substitutions accumulating during evolution.

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Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

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Peptide Mapping of Aminoacyl-tRNA Synthetases: Evidence for Internal Sequence Homology in Escherichia coli Leucyl-tRNA Synthetase

Waterson

Konigsberg

1974

Proc. Natl. Acad. Sci. U.S.A.

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“…The fusion of the standard-size early genes was perhaps a dominant factor, in which case the preferred protein sizes of "120-aa multiples (3), recurrence of methionines with that period, correspondence of the segment to the optimal DNA ring closure size (5), and correctly predicted DNA helical repeat (4) all provide a strong factual basis to the general idea of gene fusion by excision-reinsertion (7)(8)(9) and to the particular segmentation mechanism (3,4). The observed periodicities in protein sizes and in methionine distribution thus appear as fossils of those early days of protein evolution.…”

Section: Discussionmentioning

confidence: 99%

Periodic recurrence of methionines: fossil of gene fusion?

Kolker¹,

Trifonov²

1995

Proc. Natl. Acad. Sci. U.S.A.

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As we have recently shown, "20% of proteins are made of uniform size units of ;'123 aa for eukaryotes and '152 aa for prokaryotes. Such regularity may reflect certain past events in protein evolution by fusion (molecular recombination) of a spectrum of standard-size protein-coding DNA segments-the early genes. Consequently, methionines, as start residues, would mark those locations in proteins that correspond to the DNA recombination sites-the borders between the fused genes. This positional preference of the methionines may still survive as a fossil of the early protein sequence organization. In this study we address the question how methionines are distributed in modern protein sequences. This analysis of eukaryotic sequences shows that methionine residues do preferentially appear at the positions corresponding to the multiples of the unit size, as predicted.The early notion that proteins might have a standard modular structure (1) has been recently confirmed (2, 3). A welldetectable (=20%) excess of certain protein sequence sizes has been found. The preferred polypeptide chain lengths are multiples of 123 ± 3 aa for eukaryotes and 152 ± 4 aa for prokaryotes (3). Most (if not all) species and most protein types and families contribute to this general trend. The protein sequence size regularity is particularly strong among more conserved proteins (e.g., enzymes) (3). This could be taken as an indication that the observed underlying order in the protein sequence lengths is a reflection of an ancient regular organization of proteins.At some early stages, proteins might evolve by combinatorial fusion (shuffling) of genes initially of the same elementary size. It is proposed that the early genes could have been fused through molecular recombination events-insertions of the protein-coding DNA circles of certain optimal size (3, 4). The size of 300-500 bp both ensures maximal efficiency of the DNA circularization (5) and has appropriate coding capacity (100-170 aa). The recombination events-that is, insertions and deletions of the standard unit-size DNA circles-might have occurred anywhere along the sequences. However, the locations of the sites of recombination preferentially at the ends of already existing protein-coding segments would be perhaps more likely. In this case the new composite genes would carry intact component genes (segments). One consequence of the described hypothetical process of gene fusion would be the more frequent (initially perhaps strictly regular) appearance of the initiation triplets at the borders between the unit-length sequence segments. If the newly acquired methionines (initiation residues) were not in a conflict with the performance of the new recombination protein product, the presence of the methionines at the segment borders would be retained during later stages of protein evolution, and they still might be detectable in modern sequences (4). Similar behavior would be expected from termination triplets as well, or rather from mutational derivatives thereof. However, unlike...

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“…In addition, knowledge of the pa;thway would be of valule from the standpoint of biochemical evoluition, since information already obtained has revealed interesting div,ersities in genetic control and in regulation of 'the pathway in a variety of microorganisms (1,2,7).…”

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confidence: 99%

Tryptophan Biosynthesis in Cell Cultures of Nicotiana tabacum

Delmer

Mills

1968

Plant Physiol.

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(6,11).A more thorouigh understanding of the tryptophan pathway in higher planits would be utseful in view of the accepted role of tryptophan as a precursor to indoleacetic acid (12,16,20). In addition, knowledge of the pa;thway would be of valule from the standpoint of biochemical evoluition, since information already obtained has revealed interesting div,ersities in genetic control and in regulation of 'the pathway in a variety of microorganisms (1,2,7). Skoog (8). Prior to use for these experimenits, the cells were suibcul'tured at least twice at 8-day intervals in the standard medium described above, with the exception that the kinetin concentrationi was lowered 10-fold and the agar omitted. Under these conditions ithe doubling time of these cells was 2.6 days and the wet weight to dry weight ratio o,f the cells was constant. Growth was exponential throughout the entire 8-day period.

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The Evolution of an Enzyme

Cited by 45 publications

References 17 publications

Peptide Mapping of Aminoacyl-tRNA Synthetases: Evidence for Internal Sequence Homology in Escherichia coli Leucyl-tRNA Synthetase

Peptide Mapping of Aminoacyl-tRNA Synthetases: Evidence for Internal Sequence Homology in Escherichia coli Leucyl-tRNA Synthetase

Periodic recurrence of methionines: fossil of gene fusion?

Tryptophan Biosynthesis in Cell Cultures of Nicotiana tabacum

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