Proteomics Analysis for the Role of Polyphosphate in Lysinibacillus sphaericus Adaptation to Nutrition Recovery

doi:10.16409/j.cnki.2095-039x.2018.03.009

Abstract

Abstract: Though knocking out the gene ppk of polyphosphate kinase, the growth of Lysinibacillus sphaericus wild strains and ppk mutants in conditions of amino acids deficiency and nutrition recovery was investigated. In amino acid deficiency, L. sphaericus wild strains accumulated polyP, but L. sphaericus ppk mutants did not. The wild strains grew better than ppk mutants in amino acid deficiency medium and, the wild strains regained growth more quickly than ppk mutants in medium with nutrition recovery. Proteomics and bioinformatics analysis revealed that levels of PNP and RNase J protein, the components of RNA degradosome, were up-regulated in L. sphaericus ppk mutants. The regulation of mRNA stability was an important strategy for bacteria to adapt to nutrition deficiency, we suspect that L. sphaericus accumulates polyP to regulate mRNA stability and to adapt to nutritional deficiency and recovery environment.

Key words: Lysinibacillus sphaericus, polyphosphate, amino acids deficiency, environment stresses

CLC Number:

S476.1

SHI Tingyu, WANG Yuanyuan, XIANG Yubo, DONG Xinggao, Yuan Zhiming. Proteomics Analysis for the Role of Polyphosphate in Lysinibacillus sphaericus Adaptation to Nutrition Recovery[J]. journal1, 2018, 34(3): 377-387.

References

[1] Wu Y, Hu X, Ge Y, et al. Generation of mariner-based transposon insertion mutant library of Bacillus sphaericus 2297 and investigation of genes involved in sporulation and mosquito-larvicidal crystal protein synthesis[J]. FEMS Microbiology Letters, 2012, 330(2):105-112.
[2] Dalebroux Z D, Swanson M S. ppGpp:magic beyond RNA polymerase[J]. Microbiology, 2012, 10(3):203-212.
[3] Potrykus K, Cashel M. (p)ppGpp:still magical?[J]. Annual Review of Microbiology, 2008, 62:35-51.
[4] Vrentas C E, Gaal T, Berkmen M B, et al. Still looking for the magic spot:the crystallographically defined binding site for ppGpp on RNA polymerase is unlikely to be responsible for rRNA transcription regulation[J]. Journal of Molecular Biology, 2008, 377(2):551-564.
[5] Rao N N, Liu S, Kornberg A. Inorganic polyphosphate in Escherichia coli:the phosphate regulon and the stringent response[J]. Journal of Bacteriology, 1998, 180(8):2186-2193.
[6] Rao N N, Kornberg A. Inorganic polyphosphate supports resistance and survival of stationary-phase Escherichia coli[J]. Journal of Bacteriology, 1996, 178(5):1394-1400.
[7] Shiba T, Tsutsumi K, Yano H, et al. Inorganic polyphosphate and the induction of rpoS expression[J]. Proceedings of the National Academy of Sciences of the United States of America, 1997, 94(21):11210-11215.
[8] Ault-Riche D, Fraley CD, Tzeng CM, et al. Novel assay reveals multiple pathways regulating stress-induced accumulations of inorganic polyphosphate in Escherichia coli[J]. Journal of Bacteriology, 1998, 180(7):1841-1847.
[9] Shi T, Ge Y, Zhao N, et al. Polyphosphate kinase of Lysinibacillus sphaericus and its effects on accumulation of polyphosphate and bacterial growth[J]. Microbiological research, 2015, 172:41-47.
[10] Neidhardt F C, Bloch P L, Smith D F. Culture medium for enterobacteria[J]. Journal of Bacteriology, 1974, 119(3):736-747.
[11] Shi X, Rao N N, Kornberg A. Inorganic polyphosphate in Bacillus cereus:motility, biofilm formation, and sporulation[J]. Proceedings of the National Academy of Sciences of the United States of America, 2004, 101(49):17061-17065.
[12] Yuan Z, Neilsen-LeRoux C, Pasteur N, et al. Cloning and expression of the binary toxin genes of Bacillus sphaericus C3-41 in a crystal minus B. thuringiensis subsp. israelensis[J]. Acta Microbiologica Sinica, 1999, 39(1):29-35.
[13] Arantes O, Lereclus D. Construction of cloning vectors for Bacillus thuringiensis[J]. Gene, 1991, 108:115-119.
[14] Bourgouin C, Delecluse A, de la Torre F, et al. Transfer of the toxin protein genes of Bacillus sphaericus into Bacillus thuringiensis subsp. israelensis and their expression[J]. Applied and Environmental Microbiology, 1990, 56(2):340-344.
[15] Albi T, Serrano A. Inorganic polyphosphate in the microbial world. Emerging roles for a multifaceted biopolymer[J]. World Journal of Microbiology and Biotechnology, 32(2):27.
[16] Lehnik-Habrink M, Lewis R J, Mader U, et al. RNA degradation in Bacillus subtilis:an interplay of essential endo-and exoribonucleases[J]. Molecular Microbiology, 2012, 84(6):1005-1017.
[17] Schnepf E, Crickmore N, van Rie J, et al. Bacillus thuringiensis and its pesticidal crystal proteins[J]. Microbiology and Molecular Biology Reviews, 1998, 62(3):775-806.
[18] Johnson D E, McGaughey W H. Contribution of Bacillus thuringiensis spores to toxicity of purified cry proteins towards Indianmeal moth larvae[J]. Current Microbiology, 1996, 33(1):54-59.
[19] Salamitou S, Ramisse F, Brehelin M, et al. The plcR regulon is involved in the opportunistic properties of Bacillus thuringiensis and Bacillus cereus in mice and insects[J]. Microbiology, 2000, 146(11):2825-2832.
[20] Miyasono M, Inagaki S, Yamamoto M, et al. Enhancement of Delta-Endotoxin activity by toxin-free spore of Bacillus thuringiensis against the Diamondback moth, Plutella-Xylostella[J]. Journal of Invertebrate Pathology, 1994, 63(1):111-112.
[21] Donovan W P, Donovan J C, Engleman J T. Gene knockout demonstrates that vip3A contributes to the pathogenesis of Bacillus thuringiensis toward Agrotis ipsilon and Spodoptera exigua[J]. Journal of Invertebrate Pathology, 2001, 78(1):45-51.
[22] Vallet-Gely I, Lemaitre B, Boccard F. Bacterial strategies to overcome insect defences[J]. Nature Reviews Microbiology, 2008, 6(4):302-313.
[23] Azevedo C, Saiardi A. The new world of inorganic polyphosphates[J]. Biochemical Society Transactions, 2016, 44(1):13-17.
[24] Kuroda A, Murphy H, Cashel M, et al. Guanosine tetra-and pentaphosphate promote accumulation of inorganic polyphosphate in Escherichia coli[J]. The Journal of Biological Chemistry, 1997, 272(34):21240-21243.
[25] Kuroda A. A polyphosphate-lon protease complex in the adaptation of Escherichia coli to amino acid starvation Mycobacterium tuberculosis[J]. Bioscience, Biotechnology, and Biochemistry, 2006, 70(2):325-331.
[26] Sanyal S, Banerjee S K, Banerjee R, et al. Polyphosphate kinase 1, a central node in the stress response network of Mycobacterium tuberculosis, connects the two-component systems MprAB and SenX3-RegX3 and the extracytoplasmic function sigma factor, sigma E[J]. Microbiology, 2013, 159(10):2074-2086.
[27] Takayama K, Kjelleberg S. The role of RNA stability during bacterial stress responses and starvation[J]. Environmental Microbiology, 2000, 2(4):355-365.
[28] Condon C, Putzer H, Grunberg-Manago M. Processing of the leader mRNA plays a major role in the induction of thrS expression following threonine starvation in Bacillus subtilis[J]. Proceedings of the National Academy of Sciences of the United States of America, 1996, 93(14):6992-6997.
[29] Itoh H, Kawazoe Y, Shiba T. Enhancement of protein synthesis by an inorganic polyphosphate in an E. coli cell-free system[J]. Journal of Microbiological Methods, 2006, 64(2):241-249.
[30] Blum E, Py B, Carpousis A J, et al. Polyphosphate kinase is a component of the Escherichia coli RNA degradosome[J]. Molecular Microbiology, 1997, 26(2):387-398.