Mutations that alter the helix‐turn‐helix region of the spollAC protein: a Bacillus subtilis sporulation‐specific sigma factor
- 1 February 1989
- journal article
- research article
- Published by Wiley in Molecular Microbiology
- Vol. 3 (2) , 257-259
- https://doi.org/10.1111/j.1365-2958.1989.tb01815.x
Abstract
It has previously been shown that spoIIAC561, a mutation that diminishes the incidence of sporulation by more than six orders of magnitude, alters the residue at position 13 of the helix-turn-helix region of the sporulation-specific sigma factor encoded by spoIIAC from valine to methionine (Yudkin, 1987b). We have now found that four spontaneous revertants, which sporulate at an incidence of 30-60%, all contain transitions within the codon that was altered by spo-561. The mutant methionine is replaced by isoleucine in two revertants, and by threonine in the other two.This publication has 14 references indexed in Scilit:
- STRUCTURE AND FUNCTION OF BACTERIAL SIGMA FACTORSAnnual Review of Biochemistry, 1988
- Structure of the represser–operator complex of bacteriophage 434Nature, 1987
- The prediction of helix-turn-helix DNA-binding regions in proteinsProtein Engineering, Design and Selection, 1987
- Duplicated sporulation genes in bacteriaFEBS Letters, 1985
- PROTEIN-DNA RECOGNITIONAnnual Review of Biochemistry, 1984
- Protein-DNA RecognitionAnnual Review of Biochemistry, 1984
- A sporulation-induced sigma-like regulatory protein from b. subtilisCell, 1981
- Structure and conformation of amino acids containing sulfur. V. N-Formyl-L-methionineActa Crystallographica Section B: Structural Science, Crystal Engineering and Materials, 1977
- The crystal structure of glycyl-L-threonine dihydrateActa Crystallographica Section B: Structural Science, Crystal Engineering and Materials, 1973
- The crystal structure of L-isoleucineActa Crystallographica Section B: Structural Science, Crystal Engineering and Materials, 1971