PMID: 6402713Mar 10, 1983Paper

Sequence homology between Lac and Gal repressors and three sugar-binding periplasmic proteins

Nature
B Müller-Hill

Abstract

Many proteins consist of several independent folding units or domains, each specifying a different function. Repressor proteins such as Lac or lambda cI carry small N-terminal domains which recognize DNA sequences and larger C-terminal domains which are required for effector recognition and/or oligomerization. The native periplasmic metabolite-binding proteins consist of short membrane-recognizing signal sequences and larger C-terminal metabolite-binding domains which also recognize membrane-bound proteins involved in transport and chemotaxis. The DNA-recognizing domains of many repressors are homologous, as are the sugar-recognizing periplasmic proteins. Here I demonstrate that the sugar-binding domains of the Lac and Gal repressors are homologous with the sugar-binding domains of three periplasmic proteins.

References

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Citations

Jul 1, 1992·Protein Science : a Publication of the Protein Society·C A Mauzy, M A Hermodson
Aug 1, 1994·Protein Science : a Publication of the Protein Society·T M Yi, E S Lander
Aug 1, 1990·Journal of Bioenergetics and Biomembranes·C F HigginsM P Gallagher
Feb 1, 1997·Current Opinion in Structural Biology·M A KercherM Lewis
Mar 27, 2001·Protein Science : a Publication of the Protein Society·L Swint-KruseK Shive Matthews
Apr 1, 1992·Molecular Microbiology·A E Chakerian, K S Matthews
May 5, 1992·Journal of Molecular Biology·S L Mowbray, L B Cole
Mar 8, 1990·Journal of Theoretical Biology·A Slominski, R Paus
Aug 2, 1984·Nature·F A Quiocho, N K Vyas
May 5, 1985·Journal of Molecular Biology·A E ChakerianK S Matthews
May 16, 1997·The Journal of Biological Chemistry·R Horlacher, W Boos
Jun 20, 1998·Journal of Molecular Biology·A BarkerB Müller-hill
Dec 5, 1998·Journal of Molecular Biology·J MüllerB Müller-Hill

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