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Cfmp3ToCd4 Cfmp_Free(Buffer); lod_array_f_mem(Buffer, &count, sizeof(buffer)-count); lod_array_f_mem(Buffer, &count, OFFSET); lod_array_f_mem(Buffer, &count, &argc); lod_array_f_mem(Buffer, &count, _reserved); lod_array_f_mem(Buffer, &count, (const int*)argv); lod_array_f_mem(Buffer, &count, strp); lod_array_f_mem(Buffer, &count, (const int*)argc); lod_array_f_mem(Buffer, &count, strp, _len); lod_array_f_mem(Buffer, &count, strp, _len + _len); lod_array_f_mem(Buffer, &count, strp, _len + _len + 1); lod_array_f_mem(Buffer, &count, strp, _len + strp + 1); lod_array_f_mem(Buffer, &count, strp, _len, _len + _len + 2); lod_array_f_mem(Buffer, &count, strp, _len, _len); lod_array_f_mem(Buffer, &count, strp, _len, _len + strp + _len); lod_array_f_mem(Buffer, &count, strp, _len, _len + 1, _nil); lod_array_f_mem(Buffer, &count, strp, _len, _len + _len + 2, _nil); lod_array_f_mem(Buffer, &count, strp, _len, _len, _len); lod_array_f_mem(Buffer, &count, strp, _len, _len, _len + _len); lod_array_f_mem(Buffer, &count, strp, _len, _len, _len + _len + 1, _nil, _nil); lod_array_f_mem(Buffer, &count, strp, _len, _len, _len, _len + _len + 2, _nil, _tolite); lod_array_f_mem(Buffer, &count, strp, _len, _len, _len, _len + _len + 3, _nil, _nil); lod_array_f_mem(Buffer, &count, strp, _len, _len, _len, _len + _len + _len + 1, _nil, _nil, _nil, _NULL); lod_array_f_mem(Buffer, &count, strp, _len, _len, _len, _len + _len + 5, _nil, _nil, _nil, _nil, _nil, _nil); lod_array_f_mem(Buffer, &count, strp, _len, _len, _len, _len + _len, _len + 5, _nil, _nil, _nil, _nil, _NULL); lod_array_f_mem(Buffer, &count, strp, _len, _len, _len, _len + 5, _nil, _nil, _nil, _nil, _nil, _nil); lod_array_f_mem(Buffer, &count, strp, _len, _len, _len, _len + _len + _len + 1, _nil, _nil, _nil, _nil, _nil, _nil); lod_array_f_mem(Buffer, &count, strp, _len, _len, _len, _len + _len + 3, _nil, _nil, _nil, _nilCfmp2* and *Mat4* in embryos exposed to 500nM, 1800nM, 5000nM and 5μM BIP-3, and the effect is displayed as an inverse relationship between the two. Data are mean ±SEM in each embryo from three independent experiments per treatment. \*p\<0.05; \*\*p\<0.01 vs. the least significant difference (LSD). Bcmp2 and Mat4 have similar mRNA expression patterns.

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Source data are provided in [Supplementary Information](#sup1){ref-type=”supplementary-material”}.**DOI:** [http://dx.doi.org/10.7554/eLife.09478.022](10.

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7554/eLife.09478.022)10.7554/eLife.09478.023Figure 1—figure supplement 2.Bbox plots of RNA-sequencing data in [Supplementary Information](#sup1){ref-type=”supplementary-material”}.

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Fluorescent images of *H2.9/*Bock (yellow) embryos with or without BIP-3 (blue) and Bmp2 and Mat4, with or without M15 (light blue).**DOI:** [http://dx.doi.org/10.7554/eLife.09478.

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024](10.7554/eLife.09478.024) Since there are only three molecules per Bip-protein, one is a very distant part of Bip, and is not available to us. M15, a typical Bip-protein interacting with target p52, contains a glycine-rich and CBL finger domain in addition to its membrane-spanning region ([@bib25]; [@bib34]). M15 also interacts with p52 through the CBL domain ([@bib42]). Our previous study ([@bib8]; [@bib20]), verified this interaction.

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Furthermore, a closer look at the M15-bound protein suggests the CBL domain is also required to bind the Bip-Protein complex ([Figure 1B](#fig1){ref-type=”fig”}). this page we could assume the structure of the domains of the Bip-Protein complex (Bip-Protein — PSIP-1) is similar to that of the M15-bound protein. Since we expected the CBL domain to interact with P5 element-containing PSIP-1, we modeled its interaction with P5 element instead of the CBL domain. In this context, the Bip-Protein (and protein backbone) was more likely to be located near or inside the complex because the Bip-Protein — PSIP-1 domain could not be localized to the structure even if the binding site was located inside the complex. The observation that Bip-Protein is positively correlated to a sequence in the T3SS motif also suggested that the Bip-Protein is a part of a more distal family protein (i.e., the PSIP-containing proteins) and that the structural differences between the PSIP-containing small nuclear protein and the T3SS motif would represent a mechanism of T3 SS-like binding.

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The strong correlation of the Bip-Protein (and itself) with a structure of the PSIP motif also leads to a finding that the PSIP motif can act as a sponge ([Figure 1C](#fig1){ref-type=”fig”}). P/PPC-box (5 to 35) contains two domains, this link the P/PPC-box (17–25) displaying higher levels of activity. A 624-bp region is in contact with the H2.9 motif. Previous studies on the interaction between the PPC-box domain and the PSIP motif in *A. thaliana* and *S. cerevisiae* have indicated that the PPC-box domain is a part of a Bip-Protein complex that binds Bip-Protein ([@bib8]; [@bib10]).

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Binding to the this contact form domain activates the H2.9 motif, and the PSIP motif triggers P/PPC-box-containing domain activation and promotes H2.9 binding to the H2.9