The p12 domain is unstructured in a murine leukemia virus p12-CA(N) Gag construct

The Gag polyproteins of gammaretroviruses contain a conserved p12 domain between MA and CA that plays critical roles in virus assembly, reverse transcription and nuclear integration. Here we show using nuclear magnetic resonance, that p12 is unstructured in a Moloney murine leukemia virus (MMLV) Gag...

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Published inPloS one Vol. 3; no. 4; p. e1902
Main Authors Kyere, Sampson K, Joseph, Prem Raj B, Summers, Michael F
Format Journal Article
LanguageEnglish
Published United States Public Library of Science (PLoS) 02.04.2008
Subjects
Amino Acid Sequence
Capsid - chemistry
Capsid Proteins
DNA, Recombinant
Gene Products, gag - chemistry
Gene Products, gag - metabolism
Leukemia Virus, Murine - metabolism
Molecular Sequence Data
Moloney murine leukemia virus - metabolism
Protein Structure, Secondary
Protein Structure, Tertiary
Recombinant Proteins - chemistry
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Summary:The Gag polyproteins of gammaretroviruses contain a conserved p12 domain between MA and CA that plays critical roles in virus assembly, reverse transcription and nuclear integration. Here we show using nuclear magnetic resonance, that p12 is unstructured in a Moloney murine leukemia virus (MMLV) Gag fragment that includes the N-terminal domain of CA (p12-CA(N)). Furthermore, no long range interactions were observed between the domains, as has been previously predicted. Flexibility appears to be a common feature of Gag "late" domains required for virus release during budding. Residues near the N-terminus of CA(N) that form a beta-hairpin in the mature CA protein are unfolded in p12-CA(N), consistent with proposals that hairpin formation helps trigger capsid assembly.
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ISSN:1932-6203
DOI:10.1371/journal.pone.0001902