 |
PDBsum entry 5huy
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
Transport protein/viral protein
|
PDB id
|
|
|
|
5huy
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
References listed in PDB file
|
|
|
Key reference
|
|
|
Title
|
|
Divergent evolution of nuclear localization signal sequences in herpesvirus terminase subunits.
|
|
|
Authors
|
|
R.S.Sankhala,
R.K.Lokareddy,
G.Cingolani.
|
|
|
Ref.
|
|
J Biol Chem, 2016,
291,
11420-11433.
[DOI no: ]
|
|
|
PubMed id
|
|
|
|
|
|
|
|
|
Abstract
|
|
|
The tripartite terminase complex of herpesviruses assembles in the cytoplasm of
infected cells and exploits the host nuclear import machinery to gain access to
the nucleus, where capsid assembly and genome-packaging occur. Here we analyzed
the structure and conservation of nuclear localization signal (NLS) sequences
previously identified in herpes simplex virus 1 (HSV-1) large terminase and
human cytomegalovirus (HCMV) small terminase. We found a monopartite NLS at the
N terminus of large terminase, flanking the ATPase domain, that is conserved
only in α-herpesviruses. In contrast, small terminase exposes a classical NLS
at the far C terminus of its helical structure that is conserved only in two
genera of the β-subfamily and absent in α- and γ-herpesviruses. In addition,
we predicted a classical NLS in the third terminase subunit that is partially
conserved among herpesviruses. Bioinformatic analysis revealed that both
location and potency of NLSs in terminase subunits evolved more rapidly than the
rest of the amino acid sequence despite the selective pressure to keep terminase
gene products active and localized in the nucleus. We propose that swapping NLSs
among terminase subunits is a regulatory mechanism that allows different
herpesviruses to regulate the kinetics of terminase nuclear import, reflecting a
mechanism of virus:host adaptation.
|
|
|
|
|
|
|
