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Watson and Alexander Rich discussed in the PNAS, saying, "We shall not be able to check a structural relationship between RNA and protein synthesis or between RNA and DNA until we know the structure of RNA." [5] Evidences had been accumulating since the 1940s that protein synthesis occurs simultaneously with increased level of RNA in the cytoplasm.
The de novo protein synthesis theory of memory formation is a hypothesis about the formation of the physical correlates of memory in the brain. It is widely accepted that the physiological correlates for memories are stored at the synapse between various neurons .
Protein synthesis is a very similar process for both prokaryotes and eukaryotes but there are some distinct differences. [1] Protein synthesis can be divided broadly into two phases: transcription and translation. During transcription, a section of DNA encoding a protein, known as a gene, is converted into a molecule called messenger RNA (mRNA).
Memory transfer proposes a chemical basis for memory termed memory RNA which can be passed down through flesh instead of an intact nervous system. Since RNA encodes information [ 1 ] living cells produce and modify RNA in reaction to external events, it might also be used in neurons to record stimuli.
Protein synthesis plays an important role in the formation of new memories. Studies have shown that protein synthesis inhibitors administered after learning, weaken memory, suggesting that protein synthesis is required for memory consolidation. Additionally, reports have suggested that the effects of protein synthesis inhibitors also inhibit ...
Specifically, it is unclear whether protein synthesis takes place in the postsynaptic cell body or in its dendrites. [39] Despite having observed ribosomes (the major components of the protein synthesis machinery) in dendrites as early as the 1960s, prevailing wisdom was that the cell body was the predominant site of protein synthesis in ...
Regulation of protein synthesis is partly influenced by phosphorylation of eIF2 (via the α subunit), which is a part of the eIF2-GTP-Met-tRNA i Met ternary complex (eIF2-TC). When large numbers of eIF2 are phosphorylated, protein synthesis is inhibited. This occurs under amino acid starvation or after viral infection.
In analogous experiments with other synthetic RNAs, they found that poly-C directed synthesis of polyproline. Nirenberg recounts that the labs of Severo Ochoa and James Watson had earlier done similar experiments with poly-A, but failed to detect protein synthesis because polylysine (unlike most proteins) is soluble in trichloroacetic acid.