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Synthesis of H1˚ histone protein, in the developing rat brain, seems tobe regulated mainly at the post-transcriptional level. Since regulation of RNAmetabolism depends on a series of RNA-binding proteins, we have been searchingfor RNA-binding proteins involved in the post-transcriptional regulation of theH1˚ gene. We recently reported isolation, from a cDNA expression library, of aninsert encoding a novel protein, the C-terminal half of which is identical tothat of PEP-19, a brain-specific protein involved in calcium metabolism. The novelprotein was called long PEP-19 isoform (LPI). Herein we show that LPI, as wellas PEP-19, can bind H1˚ RNA. Moreover, in order to improve production of functionalLPI/PEP-19, we modified the protocol normally adopted for preparing histidinetagged-proteins from bacteria, by adding an additional purification step. We alsofound that both LPI and PEP can compete for H1˚ RNA binding with PIPPin (CSD-C2),another RNA-binding protein previously discovered in our laboratory. Since PEP19/LPIcontain a calmodulin binding domain, we finally investigated whether their abilityto bind RNA is affected by calmodulin. Our results show that calmodulin interfereswith binding of H1˚ RNA to both PEP-19 and LPI, while it is not able to bind RNAon its own. This finding suggests that calcium/calmodulin may have a role in controllingH1˚ mRNA metabolism in the developing brain.

RNA-binding activity of the rat calmodulin-binding PEP-19 protein and of the long PEP-19 isoform