Mature down cleavage
Immunex Corporation, Seattle, Washington Abstract Interleukin-1 beta IL-1 beta is derived from an inactive precursor by proteolytic cleavage. To study IL-1 beta processing, we expressed the precursor in Escherichia coli, partially purified it, and used it as a substrate for various potentially relevant protease preparations. The precursor alone was virtually inactive, but incubation with membranes from human monocytes or myeloid cell lines yielded a fold increase in IL-1 bioactivity. Western blot analysis of the incubated material showed that the 31,Da precursor is broken down to three major products, ranging from 17, to about 19, Da.
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Biological functions[ edit ] Post-translational proteolytic processing[ edit ] Limited proteolysis of a polypeptide during or after translation in protein synthesis often occurs for many proteins. The precursor to the final functional form of protein is termed proprotein , and these proproteins may be first synthesized as preproprotein. For example, albumin is first synthesized as preproalbumin and contains an uncleaved signal peptide. This forms the proalbumin after the signal peptide is cleaved, and a further processing to remove the N-terminal 6-residue propeptide yields the mature form of the protein.
CPF complex ; CPSF complex ; Cleavage and polyadenylation factor complex Complex Diagram This diagram displays the protein subunits blue of the complex and how they interact with each other. Interactions with other relevant participants such as small molecules purple , sub-complexes yellow , and other subunits red are also shown. If a participant appears in the diagram with no lines connected to it, then its specific interactions with other participants are currently unknown.
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