Predominantly buried residues in the response regulator Spo0F influence specific sensor kinase recognition.
Several alanine mutations in the response regulator Spo0F induce hypersporulation in Bacillus subtilis. L66A, I90A and H101A mutants are purported to be involved in contacts stabilizing the orientation of the alpha4-helix and hence the beta4-alpha4 kinase recognition loop. Y13A is thought to affect the orientation of the alpha1-helix and consequently phosphatase action. Using comparative NMR chemical shift analyses for these mutants, we have confirmed these suppositions and isolated residues in Spo0F critical in sensor kinases discrimination. In addition, we discuss how buried residues and intra-protein communication networks contribute to precise molecular recognition by ensuring that the correct surface is presented.
McLaughlin
Patrick D
PD
Department of Molecular & Structural Biochemistry, North Carolina State University, Raleigh, NC 27695, USA.
Bobay
Benjamin G
BG
Regel
Erin J
EJ
Thompson
Richele J
RJ
Hoch
James A
JA
Cavanagh
John
J
D000409:Alanine / Q000737:chemistry / Q000235:genetics; D000595:Amino Acid Sequence; D019943:Amino Acid Substitution; D001412:Bacillus subtilis / Q000378:metabolism / Q000502:physiology*; D001426:Bacterial Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D000071677:Histidine Kinase; D019906:Nuclear Magnetic Resonance, Biomolecular; D011487:Protein Conformation; D025941:Protein Interaction Mapping; D011494:Protein Kinases / Q000737:chemistry* / Q000378:metabolism*; D017433:Protein Structure, Secondary; D013171:Spores, Bacterial
D001426:Bacterial Proteins; C080951:Spo0F protein, Bacillus subtilis; D011494:Protein Kinases; D000071677:Histidine Kinase; D000409:Alanine