A Single Residue Unique to DinB-Like Proteins Limits Formation of the Polymerase IV Multiprotein Complex in Escherichia coli

Supplemental material

Files in this Data Supplement:

• Supplemental file 1 -

  Table S1, list of all organisms represented in the multiple-sequence alignment of DinB-like sequences

  Table S2, list of all organisms with UmuC-like sequences represented in the multiple-sequence alignment of Y-family DNA polymerases

  Fig. S1, the secondary structure of DinB(C66A) is similar to that of wild-type DinB

  Table S3, determination of secondary structure composition for DinB and DinB(C66A)

  Fig. S2, bait and prey proteins used for in vitro pulldown assays were available as relatively pure proteins

  Fig. S3, DinB and DinB(C66A) can be isolated as relatively pure proteins by hydrophobicity interaction chromatography

  Fig. S4, the 70-kDa complex obtained in the in vitro pulldown experiments contains both DinB and RecA

  Fig. S5, kinetically stable DinB(C66A)-RecA binary complexes can be disrupted by treatment with 8 M urea

  Fig. S6, native DinB contains several surface histidine residues which may mediate nonspecific binding to IMAC resin

  PDF, 855K