Lysine acetylation stabilizes SP2 protein in the silkworm Bombyx mori

Zhou, Yong; Wu, Chengcheng; Sheng, Qing; Jiang, Cheng; Chen, Qin; Lv, Zhengbing; Yao, Juming; Nie, Zhou

doi:10.1016/j.jinsphys.2016.06.008

Cited by 16 publications

(25 citation statements)

References 26 publications

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“…Transfection of the plasmid overexpressing BmApoLp‐III into BmN cells increased the survival of apoptotic cells induced by H 2 O 2 (Fig. B), and the cell survival rate increased with the increase in the transfected plasmid concentration, suggesting that BmApoLp‐III has the same antiapoptosis activity as the SP2 protein (Zhou et al ., ). Like TSA, treatment with LBH589 could decrease the survival of BmN cells due to its cell toxicity; however, this treatment could increase the survival of cells undergoing apoptosis induced by H 2 O 2 (Fig.…”

Section: Resultsmentioning

confidence: 97%

“…In our previous work, many acetylated sites were found on the nutrient storage proteins in the haemolymph of B. mori , including three storage proteins (SP1, SP2 and SP3), three apolipophorin proteins (BmApoLp‐I, BmApoLp‐II and BmApoLp‐III) and six 30 K proteins (Nie et al ., ). Furthermore, SP2, one of three storage proteins typically used for amino acids storage, was found to be stabilized by acetylation and to be quickly degraded by the decrease in acetylation level due to the competition between lysine acetylation and ubiquitination; this result suggested that acetylation may be involved in the storage and utilization of amino acids in B. mori (Zhou et al ., ). In the current work, BmApoLp‐III, one of three apolipophorin proteins typically used for lipid storage and transport (Zdybicka‐Barabas and Cytrynska, ), was further found to contain high levels of acetylation using western blotting.…”

Section: Discussionmentioning

confidence: 97%

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The effect of acetylation on the protein stability of BmApoLp‐III in the silkworm, Bombyx mori

Yang

Zhu

Liu

et al. 2019

Insect Molecular Biology

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Acetylation is an important, reversible posttranslational modification to a protein. In a previous study, we found that there were a large number of acetylated sites in various nutrient storage proteins of the silkworm haemolymph. In this study, we confirmed that acetylation can affect the stability of nutrient storage protein Bombyx mori apolipophorin‐III (BmApoLp‐III). First, the expression of BmApoLp‐III could be upregulated when BmN cells were treated with the deacetylase inhibitor panobinostat (LBH589); similarly, the expression was downregulated when the cells were treated with the acetylase inhibitor C646. Furthermore, the increase in acetylation by LBH589 could inhibit the degradation and improve the accumulation of BmApoLp‐III in BmN cells treated with cycloheximide and MG132 respectively. Moreover, we found that an increase in acetylation could decrease the ubiquitination of BmApoLp‐III and vice versa; therefore, we predicted that acetylation could improve the stability of BmApoLp‐III by competing for ubiquitination and inhibiting the protein degradation pathway mediated by ubiquitin. Additionally, BmApoLp‐III had an antiapoptosis function that increased after LBH589 treatment, which might have been due to the improved protein stability after acetylation. These results have laid the foundation for further study on the mechanism of acetylation in regulating the storage and utilization of silkworm nutrition.

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Section: Resultsmentioning

confidence: 97%

Section: Discussionmentioning

confidence: 97%

The effect of acetylation on the protein stability of BmApoLp‐III in the silkworm, Bombyx mori

Yang

Zhu

Liu

et al. 2019

Insect Molecular Biology

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“…In a previous study, we found that there are large number of lysine acetylation modifications in the nutrient storage proteins of silkworm hemolymph, including the storage proteins SP1, SP2, and SP3, 30K proteins and apolipophorin I, II, and III by nano‐HPLC/MS/MS (Nie et al, ). In addition, we found that the hemolymph nutrient storage protein SP2 and BmApoLp‐III can compete with the ubiquitin modification and block the proteasome degradation pathway mediated by ubiquitin, improving the stability and cell content of proteins (Nie et al, ; Y. Zhou et al, ). In the present work, the increase in the level of protein acetylation from the TSA treatment was accompanied by a decrease in the level of protein ubiquitination, indicating that the two processes are related.…”

Section: Discussionmentioning

confidence: 99%

“…The PCR product was then inserted into the eukaryotic expression vector pIEx‐1 to generate the recombinant vector pIEx‐1‐Bm30K‐3. The baculovirus ie1‐Bacmid system harboring an early ie1 promoter, previously constructed in our laboratory (F. Zhou et al, ), was used to express recombinant Bm30K‐3, and the recombinant ie1‐vBacmid‐Bm30K‐3 virus was constructed according to a previously described method (Y. Zhou et al, ).…”

Section: Methodsmentioning

confidence: 99%

“…The results of our previous studies have shown that there are a large number of lysine acetylated sites (Kac) present on various nutrient storage proteins, such as storage proteins (SPs), apolipophorin, and 30K proteins, in the hemolymph of B. mori . In these nutrient storage proteins, the stability of SP2 and BmApoLp‐III proteins can be regulated by acetylation modification (F. Yang et al, ; Y. Zhou et al, ). In this study, we evaluated the acetylation profiles of B. mori 30K proteins (Bm30K) in hemolymph and further assessed the effect of acetylation on Bm30K‐3.…”

Section: Introductionmentioning

confidence: 99%

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The stability and antiapoptotic activity of Bm30K‐3 can be improved by lysine acetylation in the silkworm, Bombyx mori

Liu

et al. 2019

Arch Insect Biochem Physiol

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Acetylation is an important, highly conserved, and reversible post‐translational modification of proteins. Previously, we showed by nano‐HPLC/MS/MS that many nutrient storage proteins in the silkworm are acetylated. Among these proteins, most of the known 30K proteins were shown to be acetylated, including 23 acetylated 30K proteins containing 49 acetylated sites (Kac), indicating the importance of the acetylation of 30K proteins in silkworm. In this study, Bm30K‐3, a 30K protein containing three Kac sites, was further assessed in functional studies of its acetylation. Increasing the level of Bm30K‐3 acetylation by adding the deacetylase inhibitor trichostatin A (TSA) increased the levels of this protein and further inhibited cellular apoptosis induced by H2O2. In contrast, decreasing the level of acetylation by adding the acetylase inhibitor C646 could reduce the level of Bm30K‐3 and increase H2O2‐induced apoptosis. Subsequently, BmN cells were treated with CHX and MG132, and increasing the acetylation level using TSA was shown to inhibit protein degradation and improve the stability of Bm30K‐3. Furthermore, the acetylation of Bm30K‐3 could compete with its ability to be ubiquitinated, suggesting that acetylation could inhibit the ubiquitin‐mediated proteasome degradation pathway, improving the stability and accumulation of proteins in cells. These results further indicate that acetylation might regulate nutrition storage and utilization in Bombyx mori, which requires further study.

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Cloning, expression profiling, and acetylation identification of alpha‐tubulin N‐acetyltransferase 1 from Bombyx mori

Zhou

Cheng

et al. 2018

Arch Insect Biochem Physiol

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Alpha-tubulin N-acetyltransferase 1 (ATAT1) is an acetyltransferase specific to α-tubulin and performs important functions in many cellular processes. Bombyx mori is an economic insect and also known as a model lepidoptera insect. In this study, we cloned a B. mori ATAT1 gene (BmATAT1) (Gen Bank accession number: XP_004932777.1). BmATAT1 contained an open reading frame (ORF) of 1,065 bp encoding 355 amino acids (aa). Expression profiling of BmATAT1 protein showed that the expression levels of BmATAT1 at different developmental stages and different tissues in fifth-instar larvae differ. BmATAT1 was highly expressed at the egg stage and in the head of the fifth-instar larvae. Subcellular localization showed that BmATAT1 was distributed in the cytoplasm and nucleus. Furthermore, BmATAT1 may lead to time-dependent induction of cell cycle arrest in the G2/M phase by flow cytometry analysis. Interestingly, using site-specific mutation, immunoprecipitation, and Western blotting, we further found a BmATAT1 acetylated site at K156, suggesting that this acetyltransferase could be regulated by acetylation itself.

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Lysine acetylation stabilizes SP2 protein in the silkworm Bombyx mori

Cited by 16 publications

References 26 publications

The effect of acetylation on the protein stability of BmApoLp‐III in the silkworm, Bombyx mori

The effect of acetylation on the protein stability of BmApoLp‐III in the silkworm, Bombyx mori

The stability and antiapoptotic activity of Bm30K‐3 can be improved by lysine acetylation in the silkworm, Bombyx mori

Cloning, expression profiling, and acetylation identification of alpha‐tubulin N‐acetyltransferase 1 from Bombyx mori

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