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The structure of a ribosomal protein...

Merianos, Helen J.

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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:	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. - 146 p.

Source: Dissertation Abstracts International, Volume: 65-03, Section: B, page: 1309.

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:

1017722
Chemistry, Biochemistry.

The structure of a ribosomal protein S8/spc operon mRNA complex.
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035 $a (UnM)AAI3125261
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040 $a UnM $c UnM
100 1 $a Merianos, Helen J. $3 1932498
245 1 4 $a The structure of a ribosomal protein S8/spc operon mRNA complex.
300 $a 146 p.
500 $a Source: Dissertation Abstracts International, Volume: 65-03, Section: B, page: 1309.
500 $a Director: Peter B. Moore.
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.
590 $a School code: 0265.
650 4 $a Chemistry, Biochemistry. $3 1017722
650 4 $a Biophysics, General. $3 1019105
690 $a 0487
690 $a 0786
710 2 0 $a Yale University. $3 515640
773 0 $t Dissertation Abstracts International $g 65-03B.
790 1 0 $a Moore, Peter B., $e advisor
790 $a 0265
791 $a Ph.D.
792 $a 2004
856 4 0 $u http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3125261