The ClpXP and ClpAP proteases degrade proteins with carboxy-terminal peptide tails added by the SsrA-tagging system

Article Abstract:

The cytoplasmic proteases degrade in vivo the repressor amino-terminal domain variants with carboxy-terminals. The 11-residue carboxy-terminal peptide tail is added to the nascent chain when translation is interrupted in Escherichia coli. SsrA RNA mediates this modification. The SsrA tag seems to serve as a well accepted signal for proteolysis. the implications of this tag are assessed.

Escherichia coli, Proteases, Proteolysis

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Role of the processing pore of the ClpX AAA+ ATPase in the recognition and engagement of specific protein substrates

Article Abstract:

ClpX binds substrates bearing specific classes of peptide signals denature the proteins and then translocates them through a central pore into ClpX for degradation. The results demonstrate that the ClpX pore functions in the recognition and catalytic engagement of specific substrates and recognizes different substrates classes in at last two distinct fashions.

Peptides, Properties

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Brain lipid-binding protein is a direct target of Notch signaling in radial glial cells

Article Abstract:

Radial glia functions as neural progenitors and as scaffolding supporting neuronal migration during CNS development. A study identifies brain lipid-binding protein as the first predominantly CNS-specific Notch target gene and mediates some aspects of Notch signaling in radial glia.

Central nervous system, Neuroglia, Glia

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