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PreprintCited by 5Chromosomal and Genetic VariationsRNA Interference and Gene DeliveryPlant Molecular Biology Research

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Molecular insight into the Drosophila piRNA pathway network through a combination of systematic protein interaction screening and structural prediction

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Salgania, Harpreet Kaur, Metz, Jutta, Lingren, Eric, Bleischwitz, Christian, Hauser, David, Oliveras Máté, Katalin, Bollack, Daniel, Lahr, Felix, Garbelyanski, Asen, Jeske, Mandy·2024·Nucleic Acids Research
DOI 10.1101/2024.05.31.596839PMC PMC12526068

Preprint — published as 10.1093/nar/gkaf993

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Abstract

SUMMARY: piRNA-bound PIWI proteins mediate the silencing of transposons at both the transcriptional and post-transcriptional levels, processes that are critical for genome integrity and fertility in animals. While numerous additional proteins are known to be essential for piRNA biogenesis and function in Drosophila and other animals, their molecular and mechanistic functions have remained largely unknown. To improve our molecular understanding of the Drosophila piRNA pathway, we used a cell culture-based protein-protein interaction assay called ReLo to perform a systematic pairwise interaction screen involving 22 factors operating in the cytoplasm, including PIWI proteins, Tudor domain-containing proteins (TDRDs), RNA helicases, and mitochondrial surface proteins. Through additional ReLo interaction testing and structural modeling using AlphaFold-Multimer, we have characterized six protein complexes at the molecular and structural levels. We believe that the results of this screen and our methodological approach are likely to guide future research into the molecular mechanisms underlying piRNA biogenesis and function.

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Graphical Abstract CC BY-NC · PubMed Central
Figure 1. ReLo assay-based PPI screen of cytoplasmic and mitochondrial surface piRNA pathway factors. (A) Principle of the ReLo assay. Two constructs, as indicated, were coexpressed in S2R+ cells, and an interaction between them was inferred if unanchored protein 2 relocalized to the site of membrane-anchored protein 1. Adapted from Fig. 1 of Salgania et al. [53]. (B) Summary of the PPI screen. Colored rectangles indicate PPIs identified by ReLo assays and categorized as previously characterized by crystal structures (green), previously observed in co-IPs (blue), or previously unreported (orange). Homodimer formation was not tested (gray). Boxes marked with an asterisk (*) indicate previously reported interactions based on co-IP, Y2H, CL-IP, but not crystal structures (see Supplementary Table S1) that could not be detected using the ReLo assay. Although redundant, a square layout was chosen over a triangular one to facilitate quick access to interaction partners of any given protein. (C) The interaction between Krimper and Aubergine was sDMA-dependent in ReLo assays. The interactions between Krimper and Ago3 (D) and between Papi and Piwi (E) were sDMA-independent. LLY-283 and DMSO concentrations were 0.5 μM and 0.005%, respectively, in panels (C) and (E) and 1 μM and 0.01%, respectively, in panel (D). The 4RK mutations in Aub and Ago3 were R11K/R13K/R15K/R17K and R4K/R68K/R70K/R72K, respectively. Scale bars are 10 μm. Arginine methylation of Aubergine in DMSO control samples and its absence in LLY-283-treated samples was verified by mass spectrometry (Supplementary Fig. S4).
Figure 1. ReLo assay-based PPI screen of cytoplasmic and mitochondrial surface piRNA pathway factors. (A) Principle of the ReLo assay. Two constructs, as indicated, were coexpressed in S2R+ cells, and an interaction between them was inferred if unanchored protein 2 relocalized to the site of membrane-anchored protein 1. Adapted from Fig. 1 of Salgania et al. [53]. (B) Summary of the PPI screen. Colored rectangles indicate PPIs identified by ReLo assays and categorized as previously characterized by crystal structures (green), previously observed in co-IPs (blue), or previously unreported (orange). Homodimer formation was not tested (gray). Boxes marked with an asterisk (*) indicate previously reported interactions based on co-IP, Y2H, CL-IP, but not crystal structures (see Supplementary Table S1) that could not be detected using the ReLo assay. Although redundant, a square layout was chosen over a triangular one to facilitate quick access to interaction partners of any given protein. (C) The interaction between Krimper and Aubergine was sDMA-dependent in ReLo assays. The interactions between Krimper and Ago3 (D) and between Papi and Piwi (E) were sDMA-independent. LLY-283 and DMSO concentrations were 0.5 μM and 0.005%, respectively, in panels (C) and (E) and 1 μM and 0.01%, respectively, in panel (D). The 4RK mutations in Aub and Ago3 were R11K/R13K/R15K/R17K and R4K/R68K/R70K/R72K, respectively. Scale bars are 10 μm. Arginine methylation of Aubergine in DMSO control samples and its absence in LLY-283-treated samples was verified by mass spectrometry (Supplementary Fig. S4).CC BY-NC · PubMed Central
Figure 2. Interaction between Vreteno and BoYb. (A) Domain organization of Vreteno, BoYb, and SoYb. RRM, RNA recognition motif; ZnF, zinc finger; N-RecA-like, NTD; C-RecA-like, CTD; CS, CHORD and Sgt1 domain. The asterisk indicates that the eTudor domain lacks an intact aromatic cage. (B) Vreteno binds to BoYb and SoYb in ReLo assays. (C) The NTD and the CS domains of BoYb each contribute to Vret binding. (D) The N- and C-terminal portions of Vret each contribute to BoYb binding. (E) The N-terminal part of Vret binds the NTD of BoYb and the C-terminal part of Vret binds the CS domain of BoYb. (F) AlphaFold-Multimer-generated structural model of the complex consisting of the Vret–RRM (aa 43–117) and the helicase core of BoYb (aa 38–476). The PAE plot indicates the high confidence of the prediction (see also Supplementary Fig. S6). (G) Detail of the interface formed by the Vret-RRM and the BoYb core. Residues mutated for subsequent studies are highlighted in ball-and-stick representation. (H) AlphaFold-Multimer-generated structural model of the complex consisting of the C-terminal part of Vret (aa 179–691) with the MYND domain and the eTudor domain bound to the CS domain of BoYb (aa 901–998). The PAE plot shows the high confidence of the model. (I) Detail of the interface formed by the C-terminal part of Vret and the BoYb CS domain. Residues mutated for subsequent studies are highlighted in ball-and-stick representation. (J) Combined mutations in the RRM (RRM_MUT: Y69E/M74E/Y116E) and eTudor (eTud1_MUT: Y351E/M358E) surfaces of Vret are required to abolish the BoYb interaction. (K) Mutations in both the NTD (NTD_MUT: L192E/L195E/L218E) and the CS domain (CS_MUT1: L979E/L980E/L982E) of BoYb are required to abolish the Vret interaction. Scale bars are 10 μm.
Figure 2. Interaction between Vreteno and BoYb. (A) Domain organization of Vreteno, BoYb, and SoYb. RRM, RNA recognition motif; ZnF, zinc finger; N-RecA-like, NTD; C-RecA-like, CTD; CS, CHORD and Sgt1 domain. The asterisk indicates that the eTudor domain lacks an intact aromatic cage. (B) Vreteno binds to BoYb and SoYb in ReLo assays. (C) The NTD and the CS domains of BoYb each contribute to Vret binding. (D) The N- and C-terminal portions of Vret each contribute to BoYb binding. (E) The N-terminal part of Vret binds the NTD of BoYb and the C-terminal part of Vret binds the CS domain of BoYb. (F) AlphaFold-Multimer-generated structural model of the complex consisting of the Vret–RRM (aa 43–117) and the helicase core of BoYb (aa 38–476). The PAE plot indicates the high confidence of the prediction (see also Supplementary Fig. S6). (G) Detail of the interface formed by the Vret-RRM and the BoYb core. Residues mutated for subsequent studies are highlighted in ball-and-stick representation. (H) AlphaFold-Multimer-generated structural model of the complex consisting of the C-terminal part of Vret (aa 179–691) with the MYND domain and the eTudor domain bound to the CS domain of BoYb (aa 901–998). The PAE plot shows the high confidence of the model. (I) Detail of the interface formed by the C-terminal part of Vret and the BoYb CS domain. Residues mutated for subsequent studies are highlighted in ball-and-stick representation. (J) Combined mutations in the RRM (RRM_MUT: Y69E/M74E/Y116E) and eTudor (eTud1_MUT: Y351E/M358E) surfaces of Vret are required to abolish the BoYb interaction. (K) Mutations in both the NTD (NTD_MUT: L192E/L195E/L218E) and the CS domain (CS_MUT1: L979E/L980E/L982E) of BoYb are required to abolish the Vret interaction. Scale bars are 10 μm.CC BY-NC · PubMed Central
Figure 3. Interaction between Gasz and Daed. (A) Domain organization of Gasz and Daed. SAM, sterile α motif; MLS, mitochondrial localization signal. (BandC) Daed bound to Gasz in ReLo assays. The interaction required the Zipper domain of Daed (B) and Gasz (C). An asterisk indicates that the protein (additionally) lacks the C-terminal MLS, corresponding to aa 438–461 in Gasz and aa 237–279 in Daed. The mCherry-tagged controls also contained a PH domain. (D) AlphaFold-Multimer-generated structural model of the Daed-Gasz complex (missing the MLSs). The PAE plot indicates the high confidence of the prediction (see also Supplementary Fig. S9E). (E) Detail of the interface formed by the Zipper domains of Gasz and Daed. Residues mutated for subsequent studies are highlighted in ball-and-stick representation. (F) Mutations in the Zipper interface prevented the formation of the Gasz–Daed complex. Scale bars are 10 μm.
Figure 3. Interaction between Gasz and Daed. (A) Domain organization of Gasz and Daed. SAM, sterile α motif; MLS, mitochondrial localization signal. (BandC) Daed bound to Gasz in ReLo assays. The interaction required the Zipper domain of Daed (B) and Gasz (C). An asterisk indicates that the protein (additionally) lacks the C-terminal MLS, corresponding to aa 438–461 in Gasz and aa 237–279 in Daed. The mCherry-tagged controls also contained a PH domain. (D) AlphaFold-Multimer-generated structural model of the Daed-Gasz complex (missing the MLSs). The PAE plot indicates the high confidence of the prediction (see also Supplementary Fig. S9E). (E) Detail of the interface formed by the Zipper domains of Gasz and Daed. Residues mutated for subsequent studies are highlighted in ball-and-stick representation. (F) Mutations in the Zipper interface prevented the formation of the Gasz–Daed complex. Scale bars are 10 μm.CC BY-NC · PubMed Central
Figure 4. Interaction between Armi and the Gasz–Daed complex. (A) Domain organization of Armi, Gasz, Daed, and Yb. N-RecA-like, NTD; C-RecA-like, CTD; CS, cold-shock domain; HA, helicase-associated domain, SAM, sterile α motif; MLS, mitochondrial localization signal. The asterisk indicates that the eTudor domain lacks an intact aromatic cage. (B) Armi binds to Gasz in the presence of Daed. A Gasz*–Daed fusion lacking the Gasz–MLS recruits Armi to mitochondria. (C) Armi did not bind to the Gasz-Daed fusion carrying the L359/Y396E mutation in the Gasz part (Gasz*_MUT-Daed) or the F161/I205 mutation in the Daed part (Gasz*-Daed_MUT1). (D) A Gasz–Daed fusion carrying the PH domain at the N-terminus and lacking both MLS (Gasz*–Daed*) recruited Armi to the plasma membrane. (E) The Gasz*–Daed fusion bound to the helicase core of Armi (aa 451–1168). (F) AlphaFold-Multimer-generated structural model of the Daed–Gasz complex (lacking the MLSs) bound to the helicase core (aa 451–1168) of Armi. The PAE plot showing the confidence of the prediction is depicted on the right (see also Supplementary Fig. 10C). (G) Detail of the interface formed by the CTD of Armi and the SAM domain of Daed. Residues mutated for subsequent studies are highlighted in ball-and-stick representation. (H) Mutations in the CTD–SAM interface prevented the formation of the Gasz–Daed–Armi complex. The Gasz*–Daed MUT2 is I69E/Y98E located in the Daed part and the Armi MUT_CTD is L1030E/M1061E. (I) Deletion of the Gasz Ankyrin repeat (aa 1–236) from the Gasz*–Daed fusion (Gasz*_DEL-Daed) abolished Armi binding. Mutations at the HA surface of Armi (MUT_HA, W592E/D631A) did not prevent binding to the Gasz–Daed fusion. (J) Yb interacts with Armi in ReLo assays. (K) The Armi helicase core (aa 451–1168) is necessary and sufficient for Yb binding. (L) Armi binds to the C-terminal portion (aa 335–1042) of Yb, which includes the helicase core and the eTudor domain. (M) Yb binds to the Gasz–Daed fusion in the presence of Armi. The asterisk (*) in Gasz indicates that the MLS was deleted from the protein. Scale bars are 10 μm.
Figure 4. Interaction between Armi and the Gasz–Daed complex. (A) Domain organization of Armi, Gasz, Daed, and Yb. N-RecA-like, NTD; C-RecA-like, CTD; CS, cold-shock domain; HA, helicase-associated domain, SAM, sterile α motif; MLS, mitochondrial localization signal. The asterisk indicates that the eTudor domain lacks an intact aromatic cage. (B) Armi binds to Gasz in the presence of Daed. A Gasz*–Daed fusion lacking the Gasz–MLS recruits Armi to mitochondria. (C) Armi did not bind to the Gasz-Daed fusion carrying the L359/Y396E mutation in the Gasz part (Gasz*_MUT-Daed) or the F161/I205 mutation in the Daed part (Gasz*-Daed_MUT1). (D) A Gasz–Daed fusion carrying the PH domain at the N-terminus and lacking both MLS (Gasz*–Daed*) recruited Armi to the plasma membrane. (E) The Gasz*–Daed fusion bound to the helicase core of Armi (aa 451–1168). (F) AlphaFold-Multimer-generated structural model of the Daed–Gasz complex (lacking the MLSs) bound to the helicase core (aa 451–1168) of Armi. The PAE plot showing the confidence of the prediction is depicted on the right (see also Supplementary Fig. 10C). (G) Detail of the interface formed by the CTD of Armi and the SAM domain of Daed. Residues mutated for subsequent studies are highlighted in ball-and-stick representation. (H) Mutations in the CTD–SAM interface prevented the formation of the Gasz–Daed–Armi complex. The Gasz*–Daed MUT2 is I69E/Y98E located in the Daed part and the Armi MUT_CTD is L1030E/M1061E. (I) Deletion of the Gasz Ankyrin repeat (aa 1–236) from the Gasz*–Daed fusion (Gasz*_DEL-Daed) abolished Armi binding. Mutations at the HA surface of Armi (MUT_HA, W592E/D631A) did not prevent binding to the Gasz–Daed fusion. (J) Yb interacts with Armi in ReLo assays. (K) The Armi helicase core (aa 451–1168) is necessary and sufficient for Yb binding. (L) Armi binds to the C-terminal portion (aa 335–1042) of Yb, which includes the helicase core and the eTudor domain. (M) Yb binds to the Gasz–Daed fusion in the presence of Armi. The asterisk (*) in Gasz indicates that the MLS was deleted from the protein. Scale bars are 10 μm.CC BY-NC · PubMed Central
Figure 5. The interaction between Tejas and Spindle E. (legend on next page). (A) Domain organization of Tejas and Spindle E. SIR, Spindle E-interacting region; N-RecA-like, NTD; C-RecA-like, CTD; HA, helicase-associated domain; ZnF, zinc finger. The asterisk indicates that the eTudor domain lacks an intact aromatic cage. (B) Tejas interacts with Spindle E in ReLo assays. (CandD) The interaction is mediated by the N-terminal portion of Spindle E (C) and the predominantly unstructured region of Tejas (D). (E) Multiple sequence alignment showing the SIR, which is the most conserved region of the predominantly unstructured region of Tejas and extends N-terminally of the eTudor domain. (F) The SIR of Tejas is necessary and sufficient for binding to Spindle E. (G) AlphaFold-Multimer-generated structural model of the complex formed by the helicase core of Spindle E (aa 98–773) and the C-terminal part of Tejas comprising the SIR and the eTudor domain (aa 325–559). The PAE plot indicates the confidence of the prediction (see also Supplementary Fig. S12D). (H) Detail of the interface formed by the Tejas–Spindle E complex. Residues mutated for subsequent studies are highlighted in ball-and-stick representation. (I) Mutations in the predicted interface, as indicated, prevented formation of the Tejas–Spindle E complex. Spindle E MUT is K339/V342E. (J) Spindle E bound to Qin in ReLo assays. (K) Qin bound to Tejas in the presence of Spindle E. Scale bars are 10 μm.
Figure 5. The interaction between Tejas and Spindle E. (legend on next page). (A) Domain organization of Tejas and Spindle E. SIR, Spindle E-interacting region; N-RecA-like, NTD; C-RecA-like, CTD; HA, helicase-associated domain; ZnF, zinc finger. The asterisk indicates that the eTudor domain lacks an intact aromatic cage. (B) Tejas interacts with Spindle E in ReLo assays. (CandD) The interaction is mediated by the N-terminal portion of Spindle E (C) and the predominantly unstructured region of Tejas (D). (E) Multiple sequence alignment showing the SIR, which is the most conserved region of the predominantly unstructured region of Tejas and extends N-terminally of the eTudor domain. (F) The SIR of Tejas is necessary and sufficient for binding to Spindle E. (G) AlphaFold-Multimer-generated structural model of the complex formed by the helicase core of Spindle E (aa 98–773) and the C-terminal part of Tejas comprising the SIR and the eTudor domain (aa 325–559). The PAE plot indicates the confidence of the prediction (see also Supplementary Fig. S12D). (H) Detail of the interface formed by the Tejas–Spindle E complex. Residues mutated for subsequent studies are highlighted in ball-and-stick representation. (I) Mutations in the predicted interface, as indicated, prevented formation of the Tejas–Spindle E complex. Spindle E MUT is K339/V342E. (J) Spindle E bound to Qin in ReLo assays. (K) Qin bound to Tejas in the presence of Spindle E. Scale bars are 10 μm.CC BY-NC · PubMed Central
Figure 6. The interaction between Tejas and Maelstrom or Krimper. (A) Domain organization of Tejas and Maelstrom. HMG, high mobility group box. The asterisk indicates that the eTudor domain lacks an intact aromatic cage. (B) Tejas interacts with Maelstrom in ReLo assays and the interaction is mediated by the C-terminal region of Maelstrom (aa 334–459) and the eTudor domain of Tejas (aa 334–559). (C) AlphaFold-Multimer-generated structural model of the complex formed by the eTudor domain of Tejas and the TIR of Maelstrom. Residues mutated for subsequent studies are highlighted in ball-and-stick representation. The PAE plot indicates the confidence of the prediction (see also Supplementary Fig. 13C). (D) GST pull-down assay showing binding of GST–superfolder–GFP (GsfG)–Tejas to full-length MBP–Maelstrom but not to Maelstrom lacking aa 413–459. (E) Mutations in the predicted interface prevent Tejas–Maelstrom complex formation. (F) GST pull-down assay showing binding of GST-Tejas to MBP-fused Mael C-terminus (aa 413–459) but not to a mutated version of it. (G) Domain organization of Tejas and Krimper. The asterisk indicates that the eTudor domain lacks an intact aromatic cage. (H) Tejas interacts with Krimper in ReLo assays. (I) The Krimper interaction is mediated by the eTudor domain of Tejas (aa 334–559). (J) AlphaFold-Multimer-generated structural model of the complex formed by the eTudor domain of Tejas and the TIR (aa 481–495) of Krimper. Residues mutated for subsequent studies are highlighted in ball-and-stick representation. The PAE plot indicates the confidence of the prediction (see also Supplementary Fig. 15E). (K) Mutations in the predicted Tejas interface prevented Tejas–Krimper complex formation. (L) In ReLo assays, Tejas did not bridge Krimper and Maelstrom (top panels). The Tejas–Krimper interaction is abolished by coexpression of Maelstrom (middle and lower panels). Scale bars are 10 μm.
Figure 6. The interaction between Tejas and Maelstrom or Krimper. (A) Domain organization of Tejas and Maelstrom. HMG, high mobility group box. The asterisk indicates that the eTudor domain lacks an intact aromatic cage. (B) Tejas interacts with Maelstrom in ReLo assays and the interaction is mediated by the C-terminal region of Maelstrom (aa 334–459) and the eTudor domain of Tejas (aa 334–559). (C) AlphaFold-Multimer-generated structural model of the complex formed by the eTudor domain of Tejas and the TIR of Maelstrom. Residues mutated for subsequent studies are highlighted in ball-and-stick representation. The PAE plot indicates the confidence of the prediction (see also Supplementary Fig. 13C). (D) GST pull-down assay showing binding of GST–superfolder–GFP (GsfG)–Tejas to full-length MBP–Maelstrom but not to Maelstrom lacking aa 413–459. (E) Mutations in the predicted interface prevent Tejas–Maelstrom complex formation. (F) GST pull-down assay showing binding of GST-Tejas to MBP-fused Mael C-terminus (aa 413–459) but not to a mutated version of it. (G) Domain organization of Tejas and Krimper. The asterisk indicates that the eTudor domain lacks an intact aromatic cage. (H) Tejas interacts with Krimper in ReLo assays. (I) The Krimper interaction is mediated by the eTudor domain of Tejas (aa 334–559). (J) AlphaFold-Multimer-generated structural model of the complex formed by the eTudor domain of Tejas and the TIR (aa 481–495) of Krimper. Residues mutated for subsequent studies are highlighted in ball-and-stick representation. The PAE plot indicates the confidence of the prediction (see also Supplementary Fig. 15E). (K) Mutations in the predicted Tejas interface prevented Tejas–Krimper complex formation. (L) In ReLo assays, Tejas did not bridge Krimper and Maelstrom (top panels). The Tejas–Krimper interaction is abolished by coexpression of Maelstrom (middle and lower panels). Scale bars are 10 μm.CC BY-NC · PubMed Central
Figure 7. The Tejas interaction network. (A) Tejas and its binding partners. (B) Tejas relocalized to Vasa only when Vasa carried an ATP-binding mutation that kept it in an open conformation (Vasa-open). (C) Spindle interacted with Vasa-open, Maelstrom, or Krimper when Tejas was coexpressed. (D) Maelstrom interacted with Vasa-open when Tejas was coexpressed. (E) Tejas interacted with Aubergine when Krimper was coexpressed. (F) Vasa-open interacted with Aubergine when both Tejas and Krimper were coexpressed. Coexpression of a Tejas mutant that abolishes Krimper binding (Tejas MUT, V530E/V532E) did not mediate the Vasa-open–Aub interaction. mBFP, monomeric blue fluorescent protein. Scale bars are 10 μm. (G) Summary of interactions observed in the ReLo PPI screen. Interactions are indicated by a blue connector. Proteins are grouped according to subcellular localization and colored according to protein features: PIWI proteins (green), TDRDs (orange), RNA helicases (blue), mitochondrially anchored proteins (brown), and others (gray). Note that BoYb, SoYb, and Spindle E contain both eTudor domains and RNA helicase cores.
Figure 7. The Tejas interaction network. (A) Tejas and its binding partners. (B) Tejas relocalized to Vasa only when Vasa carried an ATP-binding mutation that kept it in an open conformation (Vasa-open). (C) Spindle interacted with Vasa-open, Maelstrom, or Krimper when Tejas was coexpressed. (D) Maelstrom interacted with Vasa-open when Tejas was coexpressed. (E) Tejas interacted with Aubergine when Krimper was coexpressed. (F) Vasa-open interacted with Aubergine when both Tejas and Krimper were coexpressed. Coexpression of a Tejas mutant that abolishes Krimper binding (Tejas MUT, V530E/V532E) did not mediate the Vasa-open–Aub interaction. mBFP, monomeric blue fluorescent protein. Scale bars are 10 μm. (G) Summary of interactions observed in the ReLo PPI screen. Interactions are indicated by a blue connector. Proteins are grouped according to subcellular localization and colored according to protein features: PIWI proteins (green), TDRDs (orange), RNA helicases (blue), mitochondrially anchored proteins (brown), and others (gray). Note that BoYb, SoYb, and Spindle E contain both eTudor domains and RNA helicase cores.CC BY-NC · PubMed Central

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Metadata

Authors
Salgania, H. K., Metz, J., Lingren, E., Bleischwitz, C., Hauser, D., Oliveras Máté, K., Bollack, D., Lahr, F., Garbelyanski, A., & Jeske, M.
Affiliations
Heidelberg University (DE)
Corresponding author
Jeske, Mandy
ORCID
Venue
Nucleic Acids Research
Publisher
openRxiv
Published
2024-06-01
Volume
53
Issue
19
ISSN
0305-1048 (ISSN-L)
DOI
10.1101/2024.05.31.596839
PMC
PMC12526068
OpenAlex
W4415197847
Cited by
5
References
1
Citations by year
2026: 2 · 2025: 2 · 2024: 1
FWCI
2.16
Type
journal article
Language
en
Open access
Licence
Locations
  • Nucleic Acids Research (publishedVersion, cc-by-nc)
  • bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion, cc-by-nc-nd)
  • Europe PMC (PubMed Central) (publishedVersion, cc-by-nc)
  • PubMed (publishedVersion)
Funders
  • California Department of Fish and Game (INST 35/1503-1 FUGG, INST 35/1314-1 FUGG)
  • Deutsche Forschungsgemeinschaft (INST 35/1314-1 FUGG., INST35/1503‐1FUGG, JE827/1-1, JE-827/1-2)
  • Universität Heidelberg
  • Ministerium für Wissenschaft, Forschung und Kunst Baden-Württemberg
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Chromosomal and Genetic Variations
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA Interference and Gene Delivery
  • Life Sciences › Agricultural and Biological Sciences › Plant Science › Plant Molecular Biology Research
Keywords
piRNA pathway, PIWI proteins, piRNA biogenesis, transposon silencing, protein-protein interaction, protein complex structure, RNA helicase, Drosophila
MeSH terms
Piwi-Interacting RNA, Animals, Drosophila melanogaster, Models, Molecular, Protein Binding, RNA Helicases, Protein Interaction Mapping, Drosophila Proteins, RNA, Small Interfering, Argonaute Proteins

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