Abstract:
:Translational autocontrol of the expression of the ribosomal protein S15 proceeds through the transitory formation of a pseudoknot. A synopsis of the known data is used to propose a molecular model of the mechanism involved and for the role of the pseudoknot. This latter structure is able to recruit 30S ribosomal subunits to initiate translation, but also to bind S15 and to stop translation by trapping the ribosome on its loading site. Information on the S15 protein recognition of the messenger RNA site was deduced from mutational analyses and chemical probing. A comparison of this messenger site with the S15 ribosomal binding site was conducted by analysing hydroxyl radical footprintings of these two sites. The existence of two subsites in 16S RNA suggests that the ribosomal protein S15 might present either two different binding sites or at least one common subsite. Clues for the presence of a common site between the messenger and 16S RNA are given which cannot rule out that recognition specificity is linked to a few other determinants. Whether these determinants are different or not remains an open question.
journal_name
Biochimiejournal_title
Biochimieauthors
Bénard L,Philippe C,Ehresmann B,Ehresmann C,Portier Cdoi
10.1016/s0300-9084(96)80003-4subject
Has Abstractpub_date
1996-01-01 00:00:00pages
568-76issue
7eissn
0300-9084issn
1638-6183pii
S0300-9084(96)80003-4journal_volume
78pub_type
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