- Otan tämän 2019 uudestaan esiin Nobelin palkinnon kohdistuttua HIF säätelyyn, johon CPEB_ZZ proteiinit osallistuvat HIF1 alfa mRNA-tason säätelyllä. 10.10.2019.
J Mol Biol. 2013 Jun 12;425(11):2015-2026. doi: 10.1016/j.jmb.2013.03.009. Epub 2013 Mar 13.
The C-terminal region of cytoplasmic polyadenylation element binding protein is a ZZ domain with potential for protein-protein interactions.
Abstract
Cytoplasmic
polyadenylation element binding protein (CPEB) provides temporal and
spatial control of protein synthesis required for early development and
neuronal synaptic plasticity. CPEB regulates protein expression by
inhibiting polyadenylation of selected mRNA transcripts, which prevents
binding of the ribosome for protein synthesis. Two RNA recognition motif
domains and a C-terminal binuclear zinc-binding domain are required for
mRNA binding, but the zinc-binding domain is not required for
sequence-specific recognition of the targeted mRNA transcript. The
structure and function of the zinc-binding domain of CPEB are unknown.
The C-terminal region of CPEB may participate in assembly of the
ribonucleoprotein complex that includes the scaffold protein, Symplekin,
and the cleavage and polyadenylation specificity factor. Sumoylation of
Symplekin is required for polyadenylation, and both cleavage and
polyadenylation specificity factor and poly(A) polymerase are
sumoylated. The foreshortened poly(A) tail is maintained by poly(A)
ribonuclease, which associates with CPEB. While zinc-binding domains are
renowned for nucleic acid recognition, binuclear zinc-binding
structural motifs, such as LIM (Lin-11, Isl-1, Mec-3), RING (really
interesting new gene), PHD (plant homeodomain) and ZZ (ZZ-type zinc
finger) domains, participate in protein-protein interactions. Here, we
report the solution structure of the C-terminal zinc-binding domain of
CPEB1 (CPEB1-ZZ), which has a cross-braced zinc binding topology. The
structural similarity to other ZZ domains suggests that the CPEB1-ZZ
domain recruits sumoylated proteins during assembly of the
ribonucleoprotein complex prior to mRNA export from the nucleus.
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