Selenalysine and protein synthesis

Marco, C. De; Busiello, V.; Girolamo, M. Di; Cavallinì, D.

doi:10.1016/0005-2787(76)90232-x

Cited by 26 publications

(8 citation statements)

References 13 publications

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“…Thialysine is generally regarded as an anti-metabolite of L-lysine. Owing to its structural similarity, thialysine was reported to compete with L-lysine for activation and transfer to tRNA Lys in prokaryotes and eukaryotes [28]. In this way, the lysine analogue can be incorporated into polypeptide chains resulting in the formation of inactive proteins.…”

Section: Discussionmentioning

confidence: 99%

A novel member of the GCN5-related N-acetyltransferase superfamily from Caenorhabditis elegans preferentially catalyses the N-acetylation of thialysine [S-(2-aminoethyl)-L-cysteine]

Abo-Dalo

Ndjonka

Pinnen

et al. 2004

Biochemical Journal

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The putative diamine N-acetyltransferase D2023.4 has been cloned from the model nematode Caenorhabditis elegans. The 483 bp open reading frame of the cDNA encodes a deduced polypeptide of 18.6 kDa. Accordingly, the recombinantly expressed His6-tagged protein forms an enzymically active homodimer with a molecular mass of approx. 44000 Da. The protein belongs to the GNAT (GCN5-related N-acetyltransferase) superfamily, and its amino acid sequence exhibits considerable similarity to mammalian spermidine/spermine-N1-acetyltransferases. However, neither the polyamines spermidine and spermine nor the diamines putrescine and cadaverine were efficiently acetylated by the protein. The smaller diamines diaminopropane and ethylenediamine, as well as L-lysine, represent better substrates, but, surprisingly, the enzyme most efficiently catalyses the N-acetylation of amino acids analogous with L-lysine. As determined by the k(cat)/K(m) values, the C. elegans N-acetyltransferase prefers thialysine [S-(2-aminoethyl)-L-cysteine], followed by O-(2-aminoethyl)-L-serine and S-(2-aminoethyl)-D,L-homocysteine. Reversed-phase HPLC and mass spectrometric analyses revealed that N-acetylation of L-lysine and L-thialysine occurs exclusively at the amino moiety of the side chain. Remarkably, heterologous expression of C. elegans N-acetyltransferase D2023.4 in Escherichia coli, which does not possess a homologous gene, results in a pronounced resistance against the anti-metabolite thialysine. Furthermore, C. elegans N-acetyltransferase D2023.4 exhibits the highest homology with a number of GNATs found in numerous genomes from bacteria to mammals that have not been biochemically characterized so far, suggesting a novel group of GNAT enzymes closely related to spermidine/spermine-N1-acetyltransferase, but with a distinct substrate specificity. Taken together, we propose to name the enzyme 'thialysine N(epsilon)-acetyltransferase'.

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Section: Discussionmentioning

confidence: 99%

A novel member of the GCN5-related N-acetyltransferase superfamily from Caenorhabditis elegans preferentially catalyses the N-acetylation of thialysine [S-(2-aminoethyl)-L-cysteine]

Abo-Dalo

Ndjonka

Pinnen

et al. 2004

Biochemical Journal

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“…The first of these is the toxic lysine analog S-(2-aminoethyl)-cysteine (AEC). This analog is incorporated into proteins competitively with lysine in microbial, 160 animal, 161 and plant 162 systems. Any mutant which possesses a greater than normal pool of free lysine could be resistant by being able to dilute out the toxic analog.…”

Section: C Changes In Free Amino Acidsmentioning

confidence: 99%

Improvement of protein quality in cereals

Bright

Shewry

Kasarda

1983

Critical Reviews in Plant Sciences

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“…However, the physiological role of HsSSAT2 is still unclear. Thialysine is a structural analog of L ‐lysine, and has its role as an antimetabolite by competing with L ‐lysine for the incorporation into polypeptides, which makes proteins inactive 6, 7. Therefore, high thialysine to lysine ratios block the growth of prokaryotic and eukaryotic cells 8–11…”

Section: Introductionmentioning

confidence: 99%

Crystal structure of Homo sapiens thialysine N^ϵ‐acetyltransferase (HsSSAT2) in complex with acetyl coenzyme A

et al. 2006

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Although many studies have analyzed the causes and consequences of social relationships, few studies have explicitly assessed how measures of social relationships are affected by the choice of behaviors used to quantify them. The use of many behaviors to measure social relationships in primates has long been advocated, but it was analytically difficult to implement this framework into primatological work. However, recent advances in social network analysis (SNA) now allow the comparison of multiple networks created from different behaviors. Here we use our database of baboon social behavior (Papio anubis, Gashaka Gumti National Park, Nigeria) to investigate (i) to what extent social networks created from different behaviors overlap, (ii) to what extent individuals occupy similar social positions in these networks and (iii) how sex affects social network position in this population of baboons. We used data on grooming, aggression, displacement, mounting and presenting, which were collected over a 15‐month period. We calculated network parameters separately for each behavior. Networks based on displacement, mounting and presenting were very similar to each other, whereas grooming and aggression networks differed both from each other and from mounting, displacement and presenting networks. Overall, individual network positions were strongly affected by sex. Individuals central in one network tended to be central in most other networks as well, whereas other measures such as clustering coefficient were found to vary depending on the behavior analyzed. Thus, our results suggest that a baboon's social environment is best described by a multiplex network based on affiliative, aggressive and sexual behavior. Modern SNA provides a number of useful tools that will help us to better understand animals' social environment. We also discuss potential caveats related to their use. Am. J. Primatol. 73:775–789, 2011. © 2011 Wiley‐Liss, Inc.

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Selenalysine and protein synthesis

Cited by 26 publications

References 13 publications

A novel member of the GCN5-related N-acetyltransferase superfamily from Caenorhabditis elegans preferentially catalyses the N-acetylation of thialysine [S-(2-aminoethyl)-L-cysteine]

A novel member of the GCN5-related N-acetyltransferase superfamily from Caenorhabditis elegans preferentially catalyses the N-acetylation of thialysine [S-(2-aminoethyl)-L-cysteine]

Improvement of protein quality in cereals

Crystal structure of Homo sapiens thialysine N^ϵ‐acetyltransferase (HsSSAT2) in complex with acetyl coenzyme A

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Selenalysine and protein synthesis

Cited by 26 publications

References 13 publications

A novel member of the GCN5-related N-acetyltransferase superfamily from Caenorhabditis elegans preferentially catalyses the N-acetylation of thialysine [S-(2-aminoethyl)-L-cysteine]

A novel member of the GCN5-related N-acetyltransferase superfamily from Caenorhabditis elegans preferentially catalyses the N-acetylation of thialysine [S-(2-aminoethyl)-L-cysteine]

Improvement of protein quality in cereals

Crystal structure of Homo sapiens thialysine Nϵ‐acetyltransferase (HsSSAT2) in complex with acetyl coenzyme A

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Crystal structure of Homo sapiens thialysine N^ϵ‐acetyltransferase (HsSSAT2) in complex with acetyl coenzyme A