Structural basis of the bacteriophage TP901‐1 CI repressor dimerization and interaction with DNA. Issue 10 (13th May 2018)

• Record Type: Journal Article
• Authors: Rasmussen, Kim K.; Varming, Anders K.; Schmidt, Simon N.; Frandsen, Kristian E. H.; Thulstrup, Peter W.; Jensen, Malene Ringkjøbing; Lo Leggio, Leila
• Is Part Of: FEBS letters. Volume 592:Issue 10(2018)
• Page Start: 1738
• Page End: 1750
• Publication Date: 2018-05-13
• Subjects: dimerization domain -- helical hook motif -- phage repressor -- protein–DNA complex -- transcription factor; Biochemistry -- Periodicals; Biophysics -- Periodicals; Molecular biology -- Periodicals; Biochimie -- Périodiques; Biochemistry; Biophysics; Molecular biology; Periodicals; 572.05
• DOI: 10.1002/1873-3468.13060
• Languages: English
• ISSNs: 0014-5793

Abstract

Abstract : Temperate bacteriophages are known for their bistability, which in TP901‐1 is controlled by two proteins, CI and MOR. Clear 1 repressor (CI) is hexameric and binds three palindromic operator sites via an N‐terminal helix‐turn‐helix domain (NTD). A dimeric form, such as the truncated CI∆58 investigated here, is necessary for high‐affinity binding to DNA. The crystal structure of the dimerization region (CTD1 ) is determined here, showing that it forms a pair of helical hooks. This newly determined structure is used together with the known crystal structure of the CI‐NTD and small angle X‐ray scattering data, to determine the solution structure of CI∆58 in complex with a palindromic operator site, showing that the two NTDs bind on opposing sides of the DNA helix. Abstract :