Fine Structure of Sendai Virus Nucleocapsid

Amano, Yasuji; Takano, T; Takahashi, Kazuhiko; Ishida, Nakao

doi:10.1111/j.1348-0421.1971.tb00619.x

Japanese Journal of Microbiology

1971

DOI: 10.1111/j.1348-0421.1971.tb00619.x

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Fine Structure of Sendai Virus Nucleocapsid

Yasuji Amano¹,

T Takano²,

Kazuhiko Takahashi³

et al.

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1989

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“…The one-start helix of the nucleocapsid has been characterized both as left-handed (31) and right-handed (18) and has been previously suggested to contain either 11 or 13 NP subunits in each turn (11), 13 subunits (19), or 15 subunits (18). This helix has a pitch of about 5.0 nm in its most tightly coiled state (1,11,16,17,20,21). However, extended conformations of the nucleocapsid have been previously observed for Sendai virus (14) and for other paramyxoviruses (4,30).…”

mentioning

confidence: 99%

The Sendai virus nucleocapsid exists in at least four different helical states

Egelman¹,

Wu²,

Amrein³

et al. 1989

J Virol

164

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Sendai virus nucleocapsids have been observed by electron microscopy to coexist in three different helical pitch conformations, 5.3, 6.8, and 37.5 nm. The 5.3and 6.8-nm conformations are present both in uranyl acetate negatively stained preparations and in tantalum-tungsten metal-shadowed preparations, whereas the 37.5-nm conformation, which has not been previously reported, is present only in the shadowed preparations. The 5.3-nm pitch conformation appears to be a mixture of two discrete structural states, with a small difference in the twist of the structure between the two. We have used image reconstruction techniques on an averaged data set from eight negatively stained nucleocapsids to produce a three-dimensional reconstruction at 2.4-nm resolution of the structure in one of the 5.3-nm pitch states. There are 13.07 nucleocapsid protein (NP) subunits in each turn of the helix in this state. The helical repeat is 79.5 nm, containing 196 subunits in 15 turns of the left-handed 5.3-nm helix. The arrangement of subunits produces a 5.0-nm-diameter hollow core which forms an internal helical groove. The RNA accounts for about 3% of the mass of the nucleocapsid, and so its location is not conspicuous in the reconstruction. Because the RNA remains associated with the NP subunits during mRNA transcription and genome replication, structural transitions in the nucleocapsid may determine the accessibility of the genome to polymerases. Alternatively, the large hollow core and internal helical groove we have reconstructed may allow access to the RNA even in the tightly coiled 5.3-nm pitch conformation.

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mentioning

confidence: 99%

The Sendai virus nucleocapsid exists in at least four different helical states

Egelman¹,

Wu²,

Amrein³

et al. 1989

J Virol

164

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Fine Structure of Sendai Virus Nucleocapsid

Cited by 1 publication

References 7 publications

The Sendai virus nucleocapsid exists in at least four different helical states

The Sendai virus nucleocapsid exists in at least four different helical states

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