Title of article :
Localization of the protein L2 in the 50 S subunit and the 70 S E. coli ribosome
Author/Authors :
Regine Willumeit، نويسنده , , Stefan Forthmann، نويسنده , , J?rn Beckmann، نويسنده , , Gundo Diedrich، نويسنده , , Ralf Ratering، نويسنده , , Heinrich B Stuhrmann، نويسنده , , Knud H. Nierhaus، نويسنده ,
Issue Information :
روزنامه با شماره پیاپی سال 2001
Pages :
11
From page :
167
To page :
177
Abstract :
The protein L2 is found in all ribosomes and is one of the best conserved proteins of this mega-dalton complex. The protein was localized within both the isolated 50 S subunit and the 70 S ribosome of the Escherichia coli bacteria with the neutron-scattering technique of spin-contrast variation. L2 is elongated, exposing one end of the protein to the surface of the intersubunit interface of the 50 S subunit. The protein changes its conformation slightly when the 50 S subunit reassociates with the 30 S subunit to form a 70 S ribosome, becoming more elongated and moving approximately 30 Å into the 50 S matrix. The results support a recent observation that L2 is essential for the association of the ribosomal subunits and might participate in the binding and translocation of the tRNAs.
Keywords :
protein biosynthesis , neutron scattering , spin-contrast variation , ribosomal protein L2
Journal title :
Journal of Molecular Biology
Serial Year :
2001
Journal title :
Journal of Molecular Biology
Record number :
1240426
Link To Document :
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