Structural features and gene-expression profiles of actin homologs in Porphyra yezoensis (Rhodophyta)

Kitade, Yukihiro; Nakamura, Michiko; Uji, Toshiki; Fukuda, Satoru; Endo, Hideki; Saga, Naotsune

doi:10.1016/j.gene.2008.07.009

Cited by 11 publications

(5 citation statements)

References 52 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…During the production of fish sauce, it was assumed that GGT from fish and bacteria such as Bacillus species, Pseudomonas species, Halobacterium species, Vibrionaceae species, and Corynebacterium species, which have been reported to exist in fish sauces, were involved in the biosynthesis of γ-Glu-Val-Gly. , Since the action of proteases has been shown to occur during the fermentation of fish sauces, it is possible that Val-Gly was produced by the degradation of fish protein via proteases. A database search of the sequence of fish muscular proteins revealed that the Val-Gly sequence was present in myosin, − actin, − parvalbumin, − creatine kinase, collagen, and elastin from fish. Indeed, the Val-Gly sequences at position 6–7 of the actin-binding site-I in the myosin heavy chain, − position 342–343 of the light meromyosin domain in the myosin heavy chain, − position 45–46 of α-actin, − and position 34–35 of parvalbumin − are well conserved among various species of fish.…”

Section: Resultsmentioning

confidence: 99%

“…A database search of the sequence of fish muscular proteins revealed that the Val-Gly sequence was present in myosin, − actin, − parvalbumin, − creatine kinase, collagen, and elastin from fish. Indeed, the Val-Gly sequences at position 6–7 of the actin-binding site-I in the myosin heavy chain, − position 342–343 of the light meromyosin domain in the myosin heavy chain, − position 45–46 of α-actin, − and position 34–35 of parvalbumin − are well conserved among various species of fish. Although the existence of the Val-Gly sequence in raw fish used to make fish sauces has not been reported to date, it is possible that Val-Gly was liberated from the above protein via protease activity and then converted to γ-Glu-Val-Gly via GGT.…”

Section: Resultsmentioning

confidence: 99%

See 1 more Smart Citation

Determination and Quantification of γ-Glutamyl-valyl-glycine in Commercial Fish Sauces

Kuroda

Kato

Yamazaki

et al. 2012

J. Agric. Food Chem.

View full text Add to dashboard Cite

It was recently reported that kokumi substances such as glutathione are perceived through the calcium-sensing receptor (CaSR). In addition, screening by the CaSR assay and sensory evaluation revealed that γ-glutamyl-valyl-glycine (γ-Glu-Val-Gly) was a potent kokumi peptide. In this study, the quantities of γ-Glu-Val-Gly in various commercial fish sauces originating from Vietnam (Nuoc Mum), Thailand (Nampra), China (Yu-lu), Korea, Japan (Shottsuru and Ikanago-shoyu), and Italy (Garum) were investigated using a LC/MS/MS method followed by derivatization with 6-aminoquinoyl-N-hydroxysuccinimidyl-carbamate (AQC). The analyses revealed γ-Glu-Val-Gly at concentrations ranging from 0.04 to 1.26 mg/dL, indicating that γ-Glu-Val-Gly is widely distributed among various commercial fish sauces.

show abstract

Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

Determination and Quantification of γ-Glutamyl-valyl-glycine in Commercial Fish Sauces

Kuroda

Kato

Yamazaki

et al. 2012

J. Agric. Food Chem.

View full text Add to dashboard Cite

show abstract

“…The primers for qPCR were designed accordingly (Table , each with a ‐QF or ‐QR suffix after the name of the enzyme to indicate the orientation). A homolog of the P. yezoensis Actin2 gene ( PuACT2 ) was used as a reference with primers ACT‐QF and QCT‐QR (Kitade et al ). Total RNA was isolated from leafy thalli treated under either high (1,450 µmol m −2 s −1 ) or normal light (60 µmol m −2 s −1 ) according to Yang et al ().…”

Section: Methodsmentioning

confidence: 99%

The P450‐type carotene hydroxylase PuCHY1 from Porphyra suggests the evolution of carotenoid metabolism in red algae

Yang

Huang

et al. 2014

JIPB

View full text Add to dashboard Cite

Carotene hydroxylases catalyze the hydroxylation of a-and b-carotene hydrocarbons into xanthophylls. In red algae, b-carotene is a ubiquitously distributed carotenoid, and hydroxylated carotenoids such as zeaxanthin and lutein are also found. However, no enzyme with carotene hydroxylase activity had been previously identified in red algae. Here, we report the isolation of a gene encoding a cytochrome P450-type carotene hydroxylase (PuCHY1) from Porphyra umbilicalis, a red alga with an ancient origin. Sequence comparisons found PuCHY1 belongs to the CYP97B subfamily, which has members from different photosynthetic organisms ranging from red algae to land plants. Functional complementation in Escherichia coli suggested that PuCHY1 catalyzed the conversion from b-carotene to zeaxanthin. When we overexpressed PuCHY1 in the Arabidopsis thaliana chy2 mutant, pigment analysis showed a significant accumulation of hydroxylated carotenoids, including neoxanthin, violaxanthin, and lutein in the leaves of transgenic plants. These results confirmed a b-hydroxylation activity of PuCHY1, and also suggested a possible e-hydroxylation function. The pigment profile and gene expression analyses of the algal thallus under high-light stress suggested that P. umbilicalis is unlikely to operate a partial xanthophyll cycle for photoprotection.Keywords: Bangiales; carotene hydroxylase; carotenoid metabolism; CYP97B; cytochrome P450; Porphyra umbilicalis; red algae Citation: Yang LE, Huang XQ, Hang Y, Deng YY, Lu QQ, Lu S (2014) The P450-type carotene hydroxylase PuCHY1 from Porphyra suggested the evolution of carotenoid metabolism in red algae. J Integr Plant Biol 56: 902-915.

show abstract

“…β-actin proteins participated in much more protein–protein interactions than other proteins, and showed important roles in many cellular functions, such as the maintenance of cell motility, cell shape, and polarity to the regulation of transcription [ 3 ]. Due to β-actin ubiquitous expression in all cell types, it was used as a reference gene in Northern blot analyses, Western blot analyses, and quantitative reverse transcription polymerase chain reaction (PCR) studies [ 4 , 5 , 6 , 7 ]. Additionally, β-actin promoters have been reported to be efficient ubiquitous regulatory elements and were widely used in transgenic mammalians [ 8 ], shrimp [ 9 ], and fish [ 10 ], and they were useful tools for transgenic studies in developmental biology.…”

Section: Introductionmentioning

confidence: 99%

Functional Analysis of the Promoter Region of Japanese Flounder (Paralichthys olivaceus) β-actin Gene: A Useful Tool for Gene Research in Marine Fish

Wang

Gao

et al. 2018

IJMS

View full text Add to dashboard Cite

A newly isolated Japanese flounder (Paralichthys olivaceus) β-actin promoter and its derivative compact construct Poβ-actinΔ−1080/−801Δ−500/−201 have recently been demonstrated to promote ectopic gene expression in cell lines. Different Poβ-actin promoter deletion mutants were constructed and functionally characterized. Mutational analyses by dual-luciferase detected that three regulatory elements, including one enhancer (−1399/−1081) and two silencers (−1080/−801, −500/−201) in the first intron. The sequence located at −1399/−1081 was determined to significantly affect promoter activity. Additionally, the first exon (−1489/−1400) could also remarkably promote the β-actin promoter activity. In the following transduction application, we removed the two silencers and generated a compact reconstruct promoter/enhancer (Poβ-actinΔ−1080/−801Δ−500/−201), which exhibited relatively stronger promoter activity compared with Poβ-actin. Furthermore, the green fluorescent protein (GFP) transgenic stable flounder cell line was obtained by the reconstructed Poβ-actinΔ−1080/−801Δ−500/−201 promoter. Our study provided the potential application of Japanese flounder β-actin, particularly Poβ-actinΔ−1080/−801Δ−500/−201, in ectopic gene expression in the future.

show abstract

Structural features and gene-expression profiles of actin homologs in Porphyra yezoensis (Rhodophyta)

Cited by 11 publications

References 52 publications

Determination and Quantification of γ-Glutamyl-valyl-glycine in Commercial Fish Sauces

Determination and Quantification of γ-Glutamyl-valyl-glycine in Commercial Fish Sauces

The P450‐type carotene hydroxylase PuCHY1 from Porphyra suggests the evolution of carotenoid metabolism in red algae

Functional Analysis of the Promoter Region of Japanese Flounder (Paralichthys olivaceus) β-actin Gene: A Useful Tool for Gene Research in Marine Fish

Contact Info

Product

Resources

About