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

doi:10.1016/j.febslet.2011.11.003

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 journal › Article › peer-review

13 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 language	English
Pages (from-to)	3964-3968
Number of pages	5
Journal	FEBS Letters
Volume	585
Issue number	24
DOIs	https://doi.org/10.1016/j.febslet.2011.11.003
Publication status	Published - 2011 Dec 15

Bibliographical note

Funding Information:
This research was supported by the Basic Science Research Program through the National Research Foundation of Korea (NRF) , funded by the Ministry of Education, Science, and Technology (2010-0007445).

All Science Journal Classification (ASJC) codes

Biophysics
Structural Biology
Biochemistry
Molecular Biology
Genetics
Cell Biology

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

Access to Document

10.1016/j.febslet.2011.11.003

Cite this

@article{f9faa0cd929f419c888055acb7b8952c,

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

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.",

author = "Shin, {Youn Chul} and Chunkyu Ko and Ryu, {Wang Shick}",

note = "Funding Information: This research was supported by the Basic Science Research Program through the National Research Foundation of Korea (NRF) , funded by the Ministry of Education, Science, and Technology (2010-0007445). ",

year = "2011",

month = dec,

day = "15",

doi = "10.1016/j.febslet.2011.11.003",

language = "English",

volume = "585",

pages = "3964--3968",

journal = "FEBS Letters",

issn = "0014-5793",

publisher = "Elsevier",

number = "24",

}

TY - JOUR

T1 - Hydrophobic residues of terminal protein domain of hepatitis B virus polymerase contribute to distinct steps in viral genome replication

AU - Shin, Youn Chul

AU - Ko, Chunkyu

AU - Ryu, Wang Shick

N1 - Funding Information: This research was supported by the Basic Science Research Program through the National Research Foundation of Korea (NRF) , funded by the Ministry of Education, Science, and Technology (2010-0007445).

PY - 2011/12/15

Y1 - 2011/12/15

N2 - 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.

AB - 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.

UR - http://www.scopus.com/inward/record.url?scp=82555168210&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=82555168210&partnerID=8YFLogxK

U2 - 10.1016/j.febslet.2011.11.003

DO - 10.1016/j.febslet.2011.11.003

M3 - Article

C2 - 22079666

AN - SCOPUS:82555168210

SN - 0014-5793

VL - 585

SP - 3964

EP - 3968

JO - FEBS Letters

JF - FEBS Letters

IS - 24

ER -

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

Abstract

Bibliographical note

All Science Journal Classification (ASJC) codes

UN SDGs

Access to Document

Other files and links

Fingerprint

Cite this