Skip to main page content
U.S. flag

An official website of the United States government

Dot gov

The .gov means it’s official.
Federal government websites often end in .gov or .mil. Before sharing sensitive information, make sure you’re on a federal government site.

Https

The site is secure.
The https:// ensures that you are connecting to the official website and that any information you provide is encrypted and transmitted securely.

Access keys NCBI Homepage MyNCBI Homepage Main Content Main Navigation
. 1988 Sep;85(18):6637-41.
doi: 10.1073/pnas.85.18.6637.

Distinctive charge configurations in proteins of the Epstein-Barr virus and possible functions

Affiliations

Distinctive charge configurations in proteins of the Epstein-Barr virus and possible functions

B E Blaisdell et al. Proc Natl Acad Sci U S A. 1988 Sep.

Abstract

The protein products of several open reading frames (ORFs) of the Epstein-Barr virus (EBV) are remarkable in their distribution of charged residues. The nuclear antigen proteins EBNA1-EBNA4 of the EBV latent state contain separate significant clusters of charge of each sign. They (excepting EBNA4) also feature distinctive periodic charge patterns [e.g., (+, O)8, (O, -, -)7] and significant tandem repeats. None of the other ORFs (about 80) of the genome possess the conjunction of these properties. Only the protein encoded from BMLF1, the first immediate early transactivator protein, contains significant multiple charge clusters and periodic charge patterns. All proteins that contain significant repeats also contain at least one significant charge cluster of a single sign. These include EBNA5 and LYDMA produced during latency and BZLF1, whose expression terminates latency and initiates productive growth. It is reasonable to conclude that these aggregate significant charge configurations and repeats are important functionally for the latent existence and for the initiation of the lytic cycle and may be characteristic of these conditions. We discuss how large multimeric protein structures bound together by clusters of unlike charge may provide a mechanism for regulation of the expression of these proteins.

PubMed Disclaimer

References

    1. Biochemistry. 1974 Jan 15;13(2):211-22 - PubMed
    1. Nature. 1988 Mar 31;332(6163):464-8 - PubMed
    1. Nature. 1984 Jul 19-25;310(5974):207-11 - PubMed
    1. Nature. 1984 Nov 8-14;312(5990):121-7 - PubMed
    1. Science. 1985 Mar 8;227(4691):1238-40 - PubMed

Publication types

LinkOut - more resources