2007
DOI: 10.1021/bi7002394
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An Importin α/β-Recognized Bipartite Nuclear Localization Signal Mediates Targeting of the Human Herpes Simplex Virus Type 1 DNA Polymerase Catalytic Subunit pUL30 to the Nucleus

Abstract: Although the 1235 amino acids human herpes simplex virus type 1 (HSV-1) DNA polymerase catalytic subunit, pUL30, is essential for HSV-1 replication in the nucleus of host cells, little information is available regarding its nuclear import mechanism. The present study addresses this issue directly, characterizing pUL30's nuclear import pathway for the first time using quantitative confocal laser scanning microscopy (CLSM) on living cells, and fluorescent binding assays. In addition to a previously described nuc… Show more

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Cited by 29 publications
(48 citation statements)
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“…On the other hand, nuclear transport mechanisms of DNA polymerase catalytic subunits differ among herpesviruses. In the case of HSV-1 DNA polymerase (UL30), it was previously reported that UL30 possesses an NLS and can by itself be transferred to the nucleus, even in the absence of UL42 polymerase processivity factor (15,16,40). Also, HCMV DNA polymerase catalytic subunit (UL54) possesses an NLS in the C-terminal domain and can itself move to the nucleus (40).…”
Section: Discussionmentioning
confidence: 99%
See 1 more Smart Citation
“…On the other hand, nuclear transport mechanisms of DNA polymerase catalytic subunits differ among herpesviruses. In the case of HSV-1 DNA polymerase (UL30), it was previously reported that UL30 possesses an NLS and can by itself be transferred to the nucleus, even in the absence of UL42 polymerase processivity factor (15,16,40). Also, HCMV DNA polymerase catalytic subunit (UL54) possesses an NLS in the C-terminal domain and can itself move to the nucleus (40).…”
Section: Discussionmentioning
confidence: 99%
“…Regarding the nuclear transport mechanism of the herpesvirus DNA polymerase catalytic subunit, it was reported that UL30 of herpes simplex virus 1 (HSV-1), being complexed with its processivity factor UL42 as a holoenzyme, translocated to nuclei utilizing its own NLS (15). It was also demonstrated that nuclear translocation of HSV-1 UL30 was strongly inhibited by the inhibitors of heat shock protein 90 (Hsp90), resulting in decreased HSV-1 yields and viral DNA synthesis (16).…”
mentioning
confidence: 99%
“…Besides ssDNA binding protein, the two main complexes are a multimeric DNA polymerase holoenzyme and helicase/primase complexes. Given the high molecular weight of such proteins, their nuclear transport has been shown to be an active process mediated by a number of different IMPs, which recognize specific NLSs on the cargo proteins [52,53,54,55,56,57,58,59]. In some cases, individual subunits are capable of localizing to the cell nucleus independently of the others, like in the case of HSV and HCMV DNA polymerase holoenzyme subunits [52,53,54,55,56].…”
Section: Nuclear Transport Of Herpesviral Dna Replicating Enzymesmentioning
confidence: 99%
“…2b). However, as control, the nuclear localization of UL30NLS [29] was significantly inhibited by DN kb1 (Fig. 2a), suggesting that importin b1 played little role in the nuclear accumulation of UL79.…”
Section: Resultsmentioning
confidence: 82%