Access

You are not currently logged in.

Access your personal account or get JSTOR access through your library or other institution:

login

Log in to your personal account or through your institution.

If You Use a Screen Reader

This content is available through Read Online (Free) program, which relies on page scans. Since scans are not currently available to screen readers, please contact JSTOR User Support for access. We'll provide a PDF copy for your screen reader.

A Variant of λ Repressor with an Altered Patterned of Cooperative Binding to DNA Sites

Anna Astromoff and Mark Ptashne
Proceedings of the National Academy of Sciences of the United States of America
Vol. 92, No. 18 (Aug. 29, 1995), pp. 8110-8114
Stable URL: http://www.jstor.org/stable/2368006
Page Count: 5
  • Read Online (Free)
  • Subscribe ($19.50)
  • Cite this Item
Since scans are not currently available to screen readers, please contact JSTOR User Support for access. We'll provide a PDF copy for your screen reader.
A Variant of λ Repressor with an Altered Patterned of Cooperative Binding to DNA Sites
Preview not available

Abstract

The bacteriophage λ repressor binds cooperatively to pairs of adjacent sites in the λ chromosome, one repressor dimer binding to each site. The repressor's amino domain (that which mediates DNA binding) is connected to its carboxyl domain (that which mediates dimerization and the interaction between dimers) by a protease-sensitive linker region. We have generated a variant λ repressor that lacks this linker region. We show that dimers of the variant protein are deficient in cooperative binding to sites at certain, but not all, distances. The linker region thus extends the range over which carboxyl domains of DNA-bound dimers can interact. In particular, the linker is required for cooperative binding to a pair of sites as found in the λ chromosome, and thus is essential for the repressor's physiological function.

Page Thumbnails

  • Thumbnail: Page 
8110
    8110
  • Thumbnail: Page 
8111
    8111
  • Thumbnail: Page 
8112
    8112
  • Thumbnail: Page 
8113
    8113
  • Thumbnail: Page 
8114
    8114