title: Interaction of the isolated domain II/III of Thermus thermophilus elongation factor Tu with the nucleotide exchange factor EF-Ts.
abstract: The middle and C-terminal domain (domain II/III) of elongation factor Tu from Thermus thermophilus lacking the GTP/GDP binding domain have been prepared by treating nucleotide-free protein with Staphylococcus aureus V8 protease. The isolated domain II/III of EF-Tu has a compact structure and high resistance against tryptic treatment and thermal denaturation. As demonstrated by circular dichroism spectroscopy, the isolated domain II/III does not contain any alpha-helical structure. Nucleotide exchange factor, EF-Ts, was found to interact with domain II/III, whereas the binding of aminoacyl-tRNA, GDP and GTP to this EF-Tu fragment could not be detected.
authors: Laboratorium für Biochemie, Universität Bayreuth, FRG.
authors: M E
authors: ME
authors: Peter
authors: C O
authors: CO
authors: Reiser
authors: N K
authors: NK
authors: Schirmer
authors: T
authors: T
authors: Kiefhaber
authors: G
authors: G
authors: Ott
authors: N W
authors: NW
authors: Grillenbeck
authors: M
authors: M
authors: Sprinzl
mesh_terms: D002942:Circular Dichroism; D006153:Guanosine Diphosphate / Q000378:metabolism; D006160:Guanosine Triphosphate / Q000378:metabolism; D009691:Nucleic Acid Denaturation; D010444:Peptide Elongation Factor Tu / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism*; D010445:Peptide Elongation Factors / Q000378:metabolism*; D012346:RNA, Transfer, Amino Acyl / Q000378:metabolism; D012697:Serine Endopeptidases / Q000378:metabolism; D013696:Temperature; D013824:Thermus / Q000378:metabolism*; D014357:Trypsin / Q000378:metabolism; D014961:X-Ray Diffraction
chemical_list: D010445:Peptide Elongation Factors; D012346:RNA, Transfer, Amino Acyl; C023512:elongation factor Ts; D006153:Guanosine Diphosphate; D006160:Guanosine Triphosphate; D012697:Serine Endopeptidases; C028344:glutamyl endopeptidase; D014357:Trypsin; D010444:Peptide Elongation Factor Tu