Abstract:
:The pathway of vesicular stomatitis virus N protein from synthesis to assembly into capsids was studied by use of detergent extraction of infected HeLa cells together with protein cross-linking. One half of the newly synthesized N protein was extracted with the soluble cell proteins and, when cross-linked, never formed the N-N dimer characteristic of mature nucleocapsids. In contrast, the cytoskeleton-bound N protein first showed a diffuse spectrum of protein-protein cross-links but, after a lag of 40 min, assumed the cross-link pattern of N protein in nucleocapsids. The efficiency of forming N-N cross-linked dimers is the same for N protein on the skeleton as in nucleocapsids derived from mature virus, suggesting very similar configurations. However, the N protein bound on the skeletal framework formed several additional cross-links that were not found in mature virus and were apparently formed to cellular proteins estimated to be ca. approximately 46,000 and 60,000 in molecular weight.
journal_name
Mol Cell Bioljournal_title
Molecular and cellular biologyauthors
Chatterjee PK,Cervera MM,Penman Sdoi
10.1128/mcb.4.10.2231subject
Has Abstractpub_date
1984-10-01 00:00:00pages
2231-4issue
10eissn
0270-7306issn
1098-5549journal_volume
4pub_type
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