Importance of amino acid composition to improve skin collagen protein synthesis rates in UV-irradiated mice

AbstractAlthough protein synthesis dynamics has been studied both with theoretical models and by profiling ribosome footprints, the determinants of ribosome flux along open reading frames (ORFs) are not fully understood. Combining measurements of protein synthesis rate with ribosome footprinting data, we here inferred translation initiation and elongation rates for over a thousand ORFs in exponentially-growing wildtype yeast cells. We found that the amino acid composition of synthesized proteins is as important a determinant of translation elongation rate as parameters related to codon and tRNA adaptation. We did not find evidence of ribosome collisions curbing the protein output of yeast transcripts, either in high translation conditions associated with exponential growth, or in strains in which deletion of individual ribosomal protein genes leads to globally increased or decreased translation. Slow translation elongation is characteristic of RP-encoding transcripts, which have markedly lower protein output than other transcripts with equally high ribosome densities.Significance StatementAlthough sequencing of ribosome footprints has uncovered new aspects of mRNA translation, the determinants of ribosome flux remain incompletely understood. Combining ribosome footprint data with measurements of protein synthesis rates, we here inferred translation initiation and elongation rates for over a thousand ORFs in yeast strains with varying translation capacity. We found that the translation elongation rate varies up to ~20-fold among yeast transcripts, and is significantly correlated with the rate of translation initiation. Furthermore, the amino acid composition of synthesized proteins impacts the rate of translation elongation to the same extent as measures of codon and tRNA adaptation. Transcripts encoding ribosomal proteins are translated especially slow, having markedly lower protein output than other transcripts with equally high ribosome densities.

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Prey amino acid composition affects rates of protein synthesis and N wastage of a freshwater carnivore

Marine and Freshwater Research ◽

10.1071/mf18410 ◽

2020 ◽

Vol 71 (2) ◽

pp. 229 ◽

Cited By ~ 1

Author(s):

Georgia K. Dwyer ◽

Rick J. Stoffels ◽

Ewen Silvester ◽

Gavin N. Rees

Keyword(s):

Protein Synthesis ◽

Amino Acid ◽

Amino Acid Composition ◽

Acid Composition ◽

Energy Production ◽

Ammonia Excretion ◽

Specific Dynamic Action ◽

Fish Diet ◽

Dietary Amino Acids ◽

Ideal Protein

Humans modify prey communities and hence alter the availability of nutrients to wild carnivores. Such changes in amino acid ‘landscapes’ are likely to affect the growth of individuals, and potentially the success of populations. This study aimed to determine whether amino acid composition of animal prey alone affects protein synthesis efficiency and N wastage of a freshwater carnivore. River blackfish (Gadopsis marmoratus) were fed two diets differing only in amino acid composition: the first diet was formulated to match the composition of the fish themselves, representing a balanced ‘ideal protein’, whereas the second diet was produced to match the composition of a prey item, namely the shrimp Macrobrachium australiense. By measuring the postprandial increase in metabolic rate (specific dynamic action) and ammonia excretion, it was found that the amino acid composition of the fish diet was associated with an increase in protein synthesis, whereas the shrimp diet doubled the amount of dietary amino acids directed to pathways of catabolic energy production and N wastage. This study adds to the stoichiometric ecology literature by showing that changes in the amino acid composition of food webs could affect carnivore growth and nutrient cycling.

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Amino Acid Composition of Skin Collagen from Deep-sea Fish

The Journal of Biochemistry ◽

10.1093/oxfordjournals.jbchem.a129842 ◽

1972 ◽

Vol 71 (5) ◽

pp. 905-906 ◽

Cited By ~ 1

Author(s):

Daisaburo FUJIMOTO

Keyword(s):

Amino Acid ◽

Amino Acid Composition ◽

Acid Composition ◽

Deep Sea ◽

Skin Collagen ◽

Sea Fish

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The Anabolic Response to Plant-Based Protein Ingestion

Sports Medicine ◽

10.1007/s40279-021-01540-8 ◽

2021 ◽

Author(s):

Philippe J. M. Pinckaers ◽

Jorn Trommelen ◽

Tim Snijders ◽

Luc J. C. van Loon

Keyword(s):

Protein Synthesis ◽

Amino Acid ◽

Amino Acid Composition ◽

Acid Composition ◽

Muscle Protein ◽

Muscle Protein Synthesis ◽

Amino Acid Content ◽

Protein Source ◽

Protein Sources

AbstractThere is a global trend of an increased interest in plant-based diets. This includes an increase in the consumption of plant-based proteins at the expense of animal-based proteins. Plant-derived proteins are now also frequently applied in sports nutrition. So far, we have learned that the ingestion of plant-derived proteins, such as soy and wheat protein, result in lower post-prandial muscle protein synthesis responses when compared with the ingestion of an equivalent amount of animal-based protein. The lesser anabolic properties of plant-based versus animal-derived proteins may be attributed to differences in their protein digestion and amino acid absorption kinetics, as well as to differences in amino acid composition between these protein sources. Most plant-based proteins have a low essential amino acid content and are often deficient in one or more specific amino acids, such as lysine and methionine. However, there are large differences in amino acid composition between various plant-derived proteins or plant-based protein sources. So far, only a few studies have directly compared the muscle protein synthetic response following the ingestion of a plant-derived protein versus a high(er) quality animal-derived protein. The proposed lower anabolic properties of plant- versus animal-derived proteins may be compensated for by (i) consuming a greater amount of the plant-derived protein or plant-based protein source to compensate for the lesser quality; (ii) using specific blends of plant-based proteins to create a more balanced amino acid profile; (iii) fortifying the plant-based protein (source) with the specific free amino acid(s) that is (are) deficient. Clinical studies are warranted to assess the anabolic properties of the various plant-derived proteins and their protein sources in vivo in humans and to identify the factors that may or may not compromise the capacity to stimulate post-prandial muscle protein synthesis rates. Such work is needed to determine whether the transition towards a more plant-based diet is accompanied by a transition towards greater dietary protein intake requirements.

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