Expression and characterization of a baseplate protein for bacteriophage Mu, gp44.
The gene product of gene 44 of Mu phage (gp44) is an essential protein for baseplate assembly and has been designated as gpP, a traditional genetic assignment. The function of gp44 during the assembly or infection process is not known. In the present study, we purified the recombinant gp44 and characterized it by analytical ultracentrifugation and differential scanning microcalorimetry. The results indicate that gp44 forms a trimer comprising a complex consisting of the 42 kDa and 40 kDa subunits that had been cleaved in the C-terminal region. Thermodynamic analysis also suggested that the C-terminal region forms a flexible domain.
Kitazawa
Daisuke
D
Department of Nano-Material Systems, Graduate School of Engineering, Gunma University, 1-5-1 Tenjin-cho, Kiryu, Gunma 376-8515.
Takeda
Shigeki
S
Kageyama
Yasuhiro
Y
Tomihara
Masashi
M
Fukada
Harumi
H
D010583:Bacteriophage mu / Q000235:genetics* / Q000378:metabolism / Q000648:ultrastructure; D002152:Calorimetry, Differential Scanning; D005814:Genes, Viral; D020836:Protein Structure, Quaternary; D013816:Thermodynamics; D014461:Ultracentrifugation; D014764:Viral Proteins / Q000096:biosynthesis / Q000235:genetics* / Q000302:isolation & purification; D015678:Viral Structural Proteins / Q000235:genetics*
D014764:Viral Proteins; D015678:Viral Structural Proteins