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The structure of a ribosomal protein S8/spc operon mRNA complex

Record Type:	Electronic resources : Monograph/item
Title/Author:	The structure of a ribosomal protein S8/spc operon mRNA complex
Author:	Merianos, Helen J.
Description:	146 p.
Notes:	Director: Peter B. Moore.
Notes:	Source: Dissertation Abstracts International, Volume: 65-03, Section: B, page: 1309.
Contained By:	Dissertation Abstracts International65-03B.
Subject:	Chemistry, Biochemistry.
Online resource:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3125261
ISBN:	0496725513

The structure of a ribosomal protein S8/spc operon mRNA complex
Merianos, Helen J.

The structure of a ribosomal protein S8/spc operon mRNA complex [electronic resource] - 146 p.

Director: Peter B. Moore.

Thesis (Ph.D.)--Yale University, 2004.

In bacteria, translation of all the ribosomal protein cistrons in the spc operon mRNA is repressed by the binding of the product of one of them, S8, to an internal sequence at the 5' end of the L5 cistron. The way in which the first two genes of the spc operon are regulated, retroregulation, is mechanistically distinct from translational repression by S8 of the genes from L5 onward. A 2.8 A resolution crystal structure has been obtained of E. coli S8 bound to this site. Despite sequence differences, the structure of this complex is almost identical to that of the S8/helix 21 complex seen in the small ribosomal subunit, consistent with the hypothesis that autogeneous regulation of ribosomal protein synthesis results from conformational similarities between mRNAs and rRNAs. S8 binding must repress the translation of its own mRNA by inhibiting the formation of a ribosomal initiation complex at the start of the L5 cistron.

ISBN: 0496725513Subjects--Topical Terms:

226900
Chemistry, Biochemistry.

The structure of a ribosomal protein S8/spc operon mRNA complex
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502 $a Thesis (Ph.D.)--Yale University, 2004.
520 # $a In bacteria, translation of all the ribosomal protein cistrons in the spc operon mRNA is repressed by the binding of the product of one of them, S8, to an internal sequence at the 5' end of the L5 cistron. The way in which the first two genes of the spc operon are regulated, retroregulation, is mechanistically distinct from translational repression by S8 of the genes from L5 onward. A 2.8 A resolution crystal structure has been obtained of E. coli S8 bound to this site. Despite sequence differences, the structure of this complex is almost identical to that of the S8/helix 21 complex seen in the small ribosomal subunit, consistent with the hypothesis that autogeneous regulation of ribosomal protein synthesis results from conformational similarities between mRNAs and rRNAs. S8 binding must repress the translation of its own mRNA by inhibiting the formation of a ribosomal initiation complex at the start of the L5 cistron.
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