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The Hsp70 family of heat shock protiens contains multiple homologs ranging in size from 66-78 kDa, and are the eukaryotic equivalents of the bacterial DnaK. The most studied Hsp70 members include the cytosolic stress-induced Hsp70 (Hsp72), the constitutive cytosolic Hsc70 (Hsp73), and the ER-localized BiP (Grp78). Hsp70 family members contain highly conserved N-terminal ATP-ase and C-terminal protein binding domains. Binding of peptide to Hsp70 is assisted by Hsp40, and stimulates the inherent ATPase activity of Hsp70, facilitating ATP hydrolysis and enhanced peptide binding. Hsp70 nucleotide exchange and substrate binding coordinates the folding of newly synthesized proteins, the re-folding of misfolded or denatured proteins, coordinates trafficking of proteins across cellular membranes, inhibits protein aggregation, and targets the degradation of proteins via the proteasomal pathway.
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Western blot analysis of HSC70 (plant, ER, BiP): Lane 1: MW marker, Lane 2: Apple, Lane 3: Carrot, Lane 4: Spinach.
Analyses of sRNA-seq libraries.(A) Hierarchical clustering analysis showing the degree of similarity among the sRNA-seq libraries. Sample-to-sample distances were calculated based on log-transformed normalized read counts. The biological replicates of each sample type were highly reproducible. T: total extract; M: microsome; TP: total polysome; MBP: membrane-bound polysome; T27: sRNA-seq from total extracts in ago1-27; M27: sRNA-seq from microsomes in ago1-27. The other samples were from wild type. The numbers after the underscore represent biological replicates. (B) Size distribution of sRNAs in the indicated samples. T: total extract; M: microsome; ER-IP: ER immunoprecipitation. Note that normalization was performed against total r/t/snRNA-depleted reads. (C) The composition of sRNAs in each of three size classes. Each column represents a biological replicate. Note that normalization was performed against total r/t/snoRNA-depleted reads. (D) Western blotting using anti-GFP antibodies to show that YFP-SEC12 was in the microsomal fraction. (E) Topology mapping showing that the YFP tag of the ER transmembrane protein YFP-SEC12 was on the cytosolic side. (F) Western blotting showing that ER immunoprecipitation (using anti-GFP antibodies with the YFP-SEC12 transgenic line) contained two ER markers (YFP-SEC12 and HSC70) but not markers for Golgi (ARF1) or endosomes (SYP22). PEPC is a soluble protein. Col, wild type (without the YFP-SEC12 transgene). (G) A scatter plot showing the depletion of Pol IV-dependent siRNAs (P4siRNAs) from the microsomal fraction. Each dot represents a 100 bp window that generates P4siRNAs. Note that normalization was performed using rRNA fragments as internal controls. (H–K) Wild type and nrpd1-1 sRNA-seq samples that differ greatly in sRNA compositions were used as a proof-of-concept for the rRNA fragment-based normalization method. (H–I) Normalization using total r/tRNA-depleted, genome-matched reads led to an exaggeration of the 21-nt peak (H) and an apparent increase in the abundance of miRNAs (I) in nrpd1-1, which lacks most 24-nt siRNAs. (J–K) Normalization using rRNA fragments resulted in similar abundance of 21-nt siRNAs (J) and miRNAs (K) between wild type and nrpd1-1.DOI:http://dx.doi.org/10.7554/eLife.22750.003
Image collected and cropped by CiteAb under a CC-BY license from the following publication: Biogenesis of phased siRNAs on membrane-bound polysomes in Arabidopsis. Elife (2016)
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RUO – Research Use Only |
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| Application | ELISA, WB |
|---|---|
| Host | Goat |
| Species Reactivity | Mouse |