Hydrophobic residues of terminal protein domain of hepatitis B virus polymerase contribute to distinct steps in viral genome replication

Youn Chul Shin, Chunkyu Ko, Wang Shick Ryu

Research output: Contribution to journalArticle

11 Citations (Scopus)

Abstract

Hepatitis B virus (HBV) replicates its DNA genome via reverse transcription. Precise roles of the terminal protein domain of HBV polymerase remain unknown. To gain insight, we created alanine substitution mutations at hydrophobic residues (i.e., tyrosine, tryptophan, and isoleucine), and then examined the extent by which these mutants carry out viral genome replication. Evidence indicated that three hydrophobic residues of the terminal protein domain (i.e., W74, Y147, and Y173) contribute to distinct steps of viral genome replication: the former two residues are important for viral DNA synthesis, while the latter is important for viral RNA encapsidation.

Original languageEnglish
Pages (from-to)3964-3968
Number of pages5
JournalFEBS Letters
Volume585
Issue number24
DOIs
Publication statusPublished - 2011 Dec 15

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

Fingerprint Dive into the research topics of 'Hydrophobic residues of terminal protein domain of hepatitis B virus polymerase contribute to distinct steps in viral genome replication'. Together they form a unique fingerprint.

  • Cite this