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Interconvertibility of two chromatographically separable forms of Escherichia coli elongation factor Tu
Author(s) -
Geiser Martin,
Gordon Julian
Publication year - 1979
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(79)81264-8
Subject(s) - escherichia coli , separable space , elongation , chemistry , philosophy , stereochemistry , mathematics , biochemistry , gene , materials science , mathematical analysis , ultimate tensile strength , metallurgy
The bacterial protein synthesis elongation factor Tu (EF-Tu) has been suggested to be involved in many different cellular mechanisms. Beside its role in the translational machinery (reviewed [I]), it is a subunit of the RNA bacteriophage Q@ replicase [Z], it has also been proposed as part of the regulation mech~~m for the ribosomal RNA transc~ption [3,4]. Further, EF-Tu was suggested to have a&n-like properties [5,6] and be membrane-associated [7,8]. We showed that the EF-Tu can be separated by column chromatography on DEAE Sephadex A-50 into two different subpopulations, one of which appeared to be selectively depleted from the supernatant during sedimentation of ribosomes [9]. Moreover, two widely separated loci were found for the protein on the E. coli genome [ 101 and the gene products appear to have a different affinity for the ribosome [11,12]. This gave a rationale for the heterogeneity of the EF-Tu population. When we set out to purify further and characterize the two forms of EF-Tu, we found that they were apparently interconvertible. This and the ribosomal involvement in this interconversion is the subject of this communication,