Display Settings:

Format

Send to:

Choose Destination
Mol Cell Biol. 1999 Jul;19(7):4711-8.

Major Egr3 isoforms are generated via alternate translation start sites and differ in their abilities to activate transcription.

Author information

  • 1Departments of Neuroscience and Psychiatry and Behavioral Sciences, Johns Hopkins University School of Medicine, Baltimore, Maryland, USA.

Abstract

In previous studies, we detected a major, unidentified Egr response element (ERE) binding complex in brain extracts. We now report that this complex contains a truncated isoform of Egr3 generated by use of an alternate translation start site at methionine 106. Furthermore, the ERE binding complex previously thought to contain full-length Egr3 includes several isoforms generated by initiation at other internal methionines. Full-length and truncated (missing residues 1 to 105) Egr3 isoforms differ in the ability to stimulate transcription directed by a tandem repeat of two EREs but not by a single ERE. Taken together, our results indicate that alternative translation start sites are used to generate Egr3 isoforms with distinct transcriptional properties.

PMID:
10373520
[PubMed - indexed for MEDLINE]
PMCID:
PMC84269
Free PMC Article

Images from this publication.See all images (5)Free text

FIG. 1
FIG. 2
FIG. 3
FIG. 4
FIG. 5
PubMed Commons home

PubMed Commons

0 comments
How to join PubMed Commons

    Supplemental Content

    Icon for HighWire Icon for PubMed Central
    Loading ...
    Write to the Help Desk