Question

The mrna-bound proteome and its global occupancy profile on protein-coding transcripts

Answer 1

Protein-RNA interactions are fundamental to core biological processes, such as mRNA splicing, localization, degradation, and translation. We developed a photoreactive nucleotide-enhanced UV crosslinking and oligo(dT) purification approach to identify the mRNA-bound proteome using quantitative proteomics and to display the protein occupancy on mRNA transcripts by next-generation sequencing. Application to a human embryonic kidney cell line identified close to 800 proteins. To our knowledge, nearly one-third were not previously annotated as RNA binding, and about 15% were not predictable by computational methods to interact with RNA. Protein occupancy profiling provides a transcriptome-wide catalog of potential cis-regulatory regions on mammalian mRNAs and showed that large stretches in 3' UTRs can be contacted by the mRNA-bound proteome, with numerous putative binding sites in regions harboring disease-associated nucleotide polymorphisms. 

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Answer 2

Explanation:

Cell membrane is Bilayer, that is it is made up of two layers - inner and outer leaflet. And constituents of this layers are distributed unequally through the two surfaces to create the asymmetry. (Refer to standard textbook figure attached). This asymmetry is actually critical to cell signalling functionality. And it also reflects that the two layers have different functions. 

This phospholipid bilayer is is constantly in motion due to rotations of the bonds of the lipid. Hydrophobic tails of this bilayer locks with itself. But hydrophilic tail hydrogen bonding with water makes this group exhibit less movement as their rotation and mobility is restricted. This

structure results in increasing viscocity of the bilayer making it fluid like structure.

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