Protein Domain : RING finger protein Z, arenaviridae IPR024183

Type	Family
Description	Arenaviridae produce four gene products: RNA-directed RNA polymerase, Z (zinc finger) protein, nucleocapsid protein (NP), and envelope glycoprotein precursor (which gives rise to mature proteins GP1 and GP2). The smallest protein is the Z protein (also called p11), which has molecular size of 11 kD. The Z protein has a zinc-binding RING-finger motif. It has been suggested that the Z-protein is a structural protein and is a component of the nucleocapsid. The arenavirus RING-finger Z protein is the main driving force of arenavirus budding, and myristoylation of its N terminus plays a key role [ ]. Z proteins also possess, near their C-termini, PPxY and/or P(T/S)AP motifs. These same motifs are found in the M proteins of Ebola (and other negative stranded RNA) viruses, as well as in Gag proteins of retroviruses. They are called "late budding domains"or "L domains"(despite their short length), and are essential for viral budding. Arenaviruses do not possess the M (or matrix) protein, but the Z protein plays the same important role [ ]. The Z protein is hydrophobic and is associated with the nucleocapsid of the virion core [ ]. It has been shown to interact with several cellular proteins, including the promyelocytic leukemia protein and the eukaryote translation initiation factor 4E. The former has been proposed to contribute to the non-cytolytic nature of LCMV infection, whereas the latter has been proposed to repress cap-dependent translation. Early studies suggested a role of Z in arenavirus transcriptional regulation. However, it has been shown that Z is not required for virus RNA replication and transcription; rather, it exhibits a dose-dependent inhibitory effect on RNA synthesis mediated by the arenavirus polymerase.
Short Name	RING_finger_Z_arenaviridae