The Archaeal Signal Recognition Particle: Present Understanding and Future Perspective

Gupta, Sayandeep; Roy, Mousam; Ghosh, Abhrajyoti

doi:10.1007/s00284-016-1167-9

Cited by 6 publications

(4 citation statements)

References 110 publications

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“…This cell pellet associated radioactive count is considered as the measure of uptake of the radioactive nucleotides. The RNA used in this study was in‐vitro transcribed RNA and codes for the 7S RNA component of the archaeal signal recognition particle (SRP) (Gupta, Roy, & Ghosh, 2017). As T2‐ribonucleases are non‐specific, a non‐fungal RNA substrate was used to perform the assay.…”

Section: Resultsmentioning

confidence: 99%

Ustilago maydis secreted T2 ribonucleases, Nuc1 and Nuc2 scavenge extracellular RNA

Mukherjee

Gupta

Ghosh

et al. 2020

Cellular Microbiology

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Ustilago maydis genome codes for many secreted ribonucleases. The contribution of two among these belonging to the T2 family (Nuc1 and Nuc2) in the pathogen virulence, has been assessed in this study. The nuc1 and nuc2 deletion mutants showed not only reduced pathogenicity compared to the SG200 WT strain but also exhibited significant delay in the completion of the pathogenic lifecycle. Both the proteins were also tested for their nucleolytic activities towards RNA substrates from maize and yeast. This also yielded valuable insights into the ability of the ribonucleases to utilise extracellular RNA as a nutrient source. Our study therefore established a role of two T2 type secreted ribonucleases of a phytopathogen in the acquisition of nutrient for the first time. This study also provides evidence that maize apoplast contains RNA, which can be utilised as a substrate by both Nuc1 and Nuc2.

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Section: Resultsmentioning

confidence: 99%

Ustilago maydis secreted T2 ribonucleases, Nuc1 and Nuc2 scavenge extracellular RNA

Mukherjee

Gupta

Ghosh

et al. 2020

Cellular Microbiology

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“…To further clarify the mechanism underlying the entry of PKG II into the ER, the relationship between PKG II and signal recognition particle 54 (SRP54) was investigated. SRP54 is key to inducing newly synthesized pep-tides/aa chains to enter the ER [26]. The Co-IP results showed that PKG II could bind with SRP54 (Fig.…”

Section: Myristoylation Of Pkg II Occurs Through Modification Of G2 B...mentioning

confidence: 91%

“…Thus, several truncated forms of PKG II were constructed [i.e., PKG II-Del(3-8), Del(3-14), Del(3-20), Del(3-26), Del(3-30), Del(3-34), and Del(21-32)]. Notably, most of these truncated forms [i.e., Del(3-8), Del(3-14), Del(3-20), Del(3-26), and Del(21)(22)(23)(24)(25)(26)(27)(28)(29)(30)(31)(32)] had no obvious effect on the secretion of PKG II. However, the truncated forms Del and Del abolished the secretion of PKG II (Fig.6F), confirming that aa 3-30 were important for secre-…”

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confidence: 99%

PKG II secreted via the classical endoplasmic reticulum--Golgi apparatus secretory pathway blocks the activation of EGFR through phosporalting its threonine 406 and has an anti-tumor effect

Wu¹,

Wan²,

Wang³

et al. 2022

Front. Biosci. (Landmark Ed)

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Background: Protein kinase G type II (PKG II) is a serine/threonine-protein kinase that was originally isolated from the small intestinal mucosa with primary functions in the secretion of small intestinal mucosal cells, secretion of renin and aldosterone, and chondrocyte activities. Recent studies have shown that PKG II exerts anti-tumor effects, while a previous study by our group confirmed that PKG II inhibited the proliferation and migration of cancer cells. Interestingly, PKG II, which was typically bound to the intracellular side of the membrane, was detected in the serum and cell culture medium as a diagnostic biomarker of tumor growth. Thus, the aim of the present study was to elucidate the function and the targets of PKG II, and the mechanism underlying the secretion of this kinase. Methods: Construction of peptides and plasmids, RNA interference, Immunoelectron microscopy, Co-immunoprecipitation, N-glycosylation assay and Isolation of the Golgi apparatus were applied to investigate the secretory mechanism, and the targets and function of PKG II. Results: PKG II was secreted by enterochromaffin (EC) cells, which were components of the endocrine system in the gastrointestinal tract. Myristoylation of glycine 2 and the N-terminal sequence, especially the amino acids 3-30, acted as a signal peptide to induce the secretion of PKG II via the conventional protein secretory pathway. Moreover, recombinant PKG II inhibited the epidermal growth factor (EGF)induced activation of the EGF receptor via phosphorylating the T406 of the extracellular domain and blocked EGF-triggered proliferation of various cancer cells. Conclusions: These results revealed a correlation between the endocrine system and the secretion of protein kinase, suggesting a novel protein secretory pathway. The resuls also indicated that secreted PKG II was a potential diagnostic biomarker and an inhibitor of tumor.

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“…Archaeosome from Sulfolobus acidocaldarius was prepared by the previously described protocol (Roy et al, 2017). Briefly, S. acidocaldarius cells were grown in Brock medium at a pH of 3 and 76°C, and Bligh-Dyer method was used to isolate cell membrane.…”

Section: Preparation Of Archaeosomementioning

confidence: 99%

N-terminal helices and A domain of archaeal FtsY facilitate SRP54 binding and the association with cell membrane

Gupta

Sinha

Bhakta

et al. 2022

Preprint

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The process of protein translocation is essential to the maintenance of cellular life and has been critically addressed in eukaryotes and bacteria. However, little information is available regarding protein translocation across archaeal membranes. The signal recognition particle (SRP) plays an important role in this process. It binds the signal peptide at the N-terminus of the polypeptide chain and interacts with the cognate SRP receptor (FtsY) located on the target membrane to form a targeting complex (TC). Concomitant GTP hydrolysis by SRP and FtsY delivers the polypeptide to the adjacent protein-conducting channel. The present study aims to characterize the structural domains of FtsY contributing to the targeting complex (TC) formation in Sulfolobus acidocaldarius, a thermo-acidophilic crenarchaeon. The contacting residues between SRP54 and FtsY were mapped along the αN1-N3 helices. Interestingly, the previously reported crystal structure did not take the N-terminal A domain into account – a region rich in negatively charged residues. Such observation led us to investigate the contribution of each of the three participating helices (αN1-3) in terms of membrane association and functional TC formation. Through biophysical analyses of SRP-FtsY and FtsY-membrane interaction, and biochemical characterization of the reciprocal GTPase activity, this work sought to elucidate the minimal structural motif controlling the archaeal TC assembly.

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The Archaeal Signal Recognition Particle: Present Understanding and Future Perspective

Cited by 6 publications

References 110 publications

Ustilago maydis secreted T2 ribonucleases, Nuc1 and Nuc2 scavenge extracellular RNA

Ustilago maydis secreted T2 ribonucleases, Nuc1 and Nuc2 scavenge extracellular RNA

PKG II secreted via the classical endoplasmic reticulum--Golgi apparatus secretory pathway blocks the activation of EGFR through phosporalting its threonine 406 and has an anti-tumor effect

N-terminal helices and A domain of archaeal FtsY facilitate SRP54 binding and the association with cell membrane

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