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The Y39A mutation of HK022 Nun disrupts a boxB interaction but preserves termination activity

Title data

Burmann, Björn M. ; Uc-Mass, Augusto ; Schweimer, Kristian ; Gottesman, Max E. ; Rösch, Paul:
The Y39A mutation of HK022 Nun disrupts a boxB interaction but preserves termination activity.
In: Biochemistry. Vol. 47 (2008) Issue 28 . - pp. 7335-7341.
ISSN 1520-4995
DOI: https://doi.org/10.1021/bi8004347

Abstract in another language

Coliphage HK022 Nun protein targets phage lambda nut boxB RNA and acts as a transcriptional terminator, counteracting the phage lambda N protein, a suppressor of transcription termination. Both Nun and N protein interact directly with RNA polymerase, and Nun competes with N protein for boxB binding and prevents superinfection of Escherichia coli HK022 lysogens by lambda. Interaction of Trp18 of lambda N and A7 of boxB RNA in the N- boxB complex is essential for efficient antitermination. We found that the corresponding Nun mutation, Nun Y39A, disrupts the interaction between the aromatic ring of Y39 and A7, but the mutant retains in vivo termination activity. Stabilization of the complex by interaction of A7 with an aromatic amino acid is thus less important for Nun activity than it is for N activity. Structural investigations show similar binding of mutant and wild-type (wt) Nun protein to boxB RNA. The dissociation constants of the wt Nun(20-44)- boxB and mutant Nun(20-44)- boxB complex as well as the structures of the boxB RNA in both complexes are identical.

Further data

Item Type: Article in a journal
Refereed: Yes
Institutions of the University: Faculties
Faculties > Faculty of Biology, Chemistry and Earth Sciences
Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry
Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry > Former Professors
Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry > Chair Biopolymers
Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry > Former Professors > Chair Biopolymers - Univ.-Prof. Dr. Paul Rösch
Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry > Chair Biopolymers > Lehrstuhl Biopolymere - Apl. Prof. Dr. Birgitta Wöhrl
Result of work at the UBT: Yes
DDC Subjects: 500 Science > 540 Chemistry
500 Science > 570 Life sciences, biology
Date Deposited: 30 Jan 2019 10:41
Last Modified: 12 Jun 2019 08:24
URI: https://eref.uni-bayreuth.de/id/eprint/47129