Skip NavigationSkip to Content
Return Return to Search Results

Targeting to the endoplasmic reticulum improves the folding of recombinant human telomerase reverse transcriptase

  1. Author:
    Wu, C. K.
    Gousset, K.
    Hughes, S. H.

  2. Author Address

    NCI, HIV Drug Resistance Program, Frederick, MD 21702 USA.;Hughes, SH, NCI, HIV Drug Resistance Program, POB B,Bldg 539,Room 130A, Frederick, MD 21702 USA.;hughes@ncifcrf.gov
    1. Year: 2007
    2. Date: Nov
  2. Journal: Protein Expression and Purification
    1. 56
    2. 1
    3. Pages: 8-19
  4. Type of Article: Article
  5. ISSN: 1046-5928
  1. Abstract:

    Telomerase is a specialized reverse transcriptase that catalyzes the addition of telomeric repeats, TTAGGG in all vertebrates, to the ends of chromosomes. The lack of recombinant purified human telomerase reverse transcriptase (hTERT) has hampered biochemical and structural studies. The primary problem in generating active recombinant hTERT appears to be protein folding, which may be due to the fact that telomerase is a multi-component ribonucleoprotein complex. When expressed in most heterologous systems, recombinant hTERT is largely insoluble. Here we describe a protein expression system using a baculovirus vector that can be used to prepare properly folded, enzymatically active, hTERT. In this system, the recombinant hTERT is directed to the endoplasmic reticulum (ER), which is rich in chaperones. This increases the expression of soluble recombinant hTERT, promoting proper folding using intrinsic ER chaperone proteins. Published by Elsevier Inc.

    See More

  1. Keywords:

External Sources

  1. View Full Text
  2. DOI: 10.1016/j.pep.2007.05.016
  3. View record in Web of Science®
  4. WOS: 000250639100002

Library Notes

  1. No notes added.
NCI at Frederick

You are leaving a government website.

This external link provides additional information that is consistent with the intended purpose of this site. The government cannot attest to the accuracy of a non-federal site.

Linking to a non-federal site does not constitute an endorsement by this institution or any of its employees of the sponsors or the information and products presented on the site. You will be subject to the destination site's privacy policy when you follow the link.

ContinueCancel