This study describes a polymerase chain reaction (PCR)-based approach, which without knowing the history of a forensic sample, is able to reveal whether the source of the sample is human or animal, and, if animal, which of the 221 animal species included in the study, simply by using one set of novel primers to amplify and sequence the PCR amplicons. The primers described in this study universally amplify a specific segment of mitochondrial cytochrome b sequence from a sample of unknown origin and delineate its identity to the level of family, genus and species. Because these primers are universal, this approach can be applied to an enormous number of other species, which are not included in the study, and could be an ultimate solution for the identification of species for forensic application.

Ras association domain family 1A (RASSF1A) is a tumour suppressor that contains an amino-terminal cysteine-rich region, similar to the diacylglycerol (DAG)-binding domain (C1 domain) found in the protein kinase C (PKC) family of proteins, and a carboxy-terminal Ras-association (RA) domain. In the present study, RASSF1A was identified as a substrate for PKC. Using classical biochemical approaches, it was established that S197 and S203 within the RA domain of RASSF1A are phosphorylated by PKC in vitro and in vivo. Unlike the WT protein, the S197, 203D double mutant of RASSF1A failed to modulate microtubule organization and perinuclear vimentin collapse. By contrast, the equivalent AA mutant of RASSF1A phenocopied the WT protein. These findings indicate that PKC phosphorylation of RASSF1A regulates its ability to reorganize the microtubule network.

No abstract