FEBS Letters
Volume 584, Issue 4 , Pages 675-680, 19 February 2010

The N-terminal domain of human holocarboxylase synthetase facilitates biotinylation via direct interaction with the substrate protein

Edited by Gianni Cesareni

  • Chung-Kyung Lee
    • ,
  • Chaejoon Cheong

      Affiliations

    • Corresponding Author InformationCorresponding authors. Address: Division of Magnetic Resonance Research, Korea Basic Science Institute, 804-1 Yangcheong-Ri, Ochang-Eup, Cheongwon-Gun, Chungbuk 363-883, Republic of Korea. Fax: +82 43 240 5059.
    • ,
  • Young Ho Jeon

      Affiliations

    • Corresponding Author InformationCorresponding authors. Address: Division of Magnetic Resonance Research, Korea Basic Science Institute, 804-1 Yangcheong-Ri, Ochang-Eup, Cheongwon-Gun, Chungbuk 363-883, Republic of Korea. Fax: +82 43 240 5059.

Division of Magnetic Resonance Research, Korea Basic Science Institute, 804-1 Yangcheong-Ri, Ochang-Eup, Cheongwon-Gun, Chungbuk 363-883, Republic of Korea

Bio-Analytical Science Program, University of Science and Technology, Daejeon 350-333, Republic of Korea

Received 10 November 2009; received in revised form 21 December 2009; accepted 26 December 2009. published online 18 January 2010.

Abstract 

Human holocarboxylase synthetase shows a high degree of sequence homology in the catalytic domain with bacterial biotin ligases such as Escherichia coli BirA, but differs in the length and sequence of the N-terminus. Despite several studies having been undertaken on the N-terminal region of hHCS, the role of this region remains unclear. We determined the structure of the N-terminal domain of hHCS by limited proteolysis and showed that this domain has a crucial effect on the enzymatic activity. The domain interacts not only with biotin acceptor protein, but also with the catalytic domain of hHCS, as shown by nuclear magnetic resonance (NMR) experiments. We propose that the N-terminal domain of hHCS recognizes the charged region of biotin acceptor protein, distinctly from the recognition by the catalytic domain.

Structured summary

MINT-7543113: hHCS (uniprotkb:P50747) and hHCS (uniprotkb:P50747) bind (MI:0407) by nuclear magnetic resonance (MI:0077)

MINT-7543096, MINT-7543129: ACC75 (uniprotkb:O00763) and hHCS (uniprotkb:P50747) bind (MI:0407) by nuclear magnetic resonance (MI:0077)

MINT-7543053: hHCS (uniprotkb:P50747) enzymaticly reacts (MI:0414) ACC75 (uniprotkb:O00763) by nuclear magnetic resonance (MI:0077)

MINT-7543070: hHCS (uniprotkb:P50747) enzymaticly reacts (MI:0414) ACC75 (uniprotkb:O00763) by enzymatic study (MI:0415)

Abbreviations: BPL, biotin protein ligase, CSP, chemical shift perturbation, HCS, holocarboxylase synthetase, HSQC, heteronuclear single quantum coherence, NMR, nuclear magnetic resonance

Keywords: Holocarboxylase synthetase, Acetyl-CoA carboxylase, Biotinoyl domain, Biotinylation, Avidin blot

To access this article, please choose from the options below

Login to an existing account or Register a new account.

  • Purchase this article for 31.50 USD (You must login/register to purchase this article)

    Online access for 24 hours. The PDF version can be downloaded as your permanent record.

  • Subscribe to this title

    Get unlimited online access to this article and all other articles in this title 24/7 for one year.

  • Claim access now

    For current subscribers with Society Membership or Account Number.

  • Visit SciVerse ScienceDirect to see if you have access via your institution.
 

PII: S0014-5793(10)00047-5

doi:10.1016/j.febslet.2009.12.059

FEBS Letters
Volume 584, Issue 4 , Pages 675-680, 19 February 2010

Article Tools

* Image Usage & Resolution