Detailed Information on Publication Record

NORTH, O.I., K. SAKAI, E. YAMASHITA, A. NAKAGAWA, T. IWAZAKI, Carina Renate BÜTTNER, S. TAKEDA and A.R. DAVIDSON. Phage tail fibre assembly proteins employ a modular structure to drive the correct folding of diverse fibres. Nature Microbiology. London: Nature Publishing Group, 2019, vol. 4, No 10, p. 1645-1653. ISSN 2058-5276. Available from: https://dx.doi.org/10.1038/s41564-019-0477-7.

Other formats: BibTeX LaTeX RIS

TY  - JOUR
ID  - 1635282
AU  - North, O.I. - Sakai, K. - Yamashita, E. - Nakagawa, A. - Iwazaki, T. - Büttner, Carina Renate - Takeda, S. - Davidson, A.R.
PY  - 2019
TI  - Phage tail fibre assembly proteins employ a modular structure to drive the correct folding of diverse fibres
JF  - Nature Microbiology
VL  - 4
IS  - 10
SP  - 1645-1653
EP  - 1645-1653
PB  - Nature Publishing Group
SN  - 20585276
KW  - EVEN-TYPE BACTERIOPHAGES
KW  - CELL-WALL RECEPTOR
KW  - HOST-RANGE
KW  - BINDING
KW  - DOMAIN
KW  - SPECIFICITY
KW  - COMPONENTS
UR  - http://dx.doi.org/10.1038/s41564-019-0477-7
L2  - http://dx.doi.org/10.1038/s41564-019-0477-7
N2  - Phage tail fibres are elongated protein assemblies capable of specific recognition of bacterial surfaces during the first step of viral infection(1-4). The folding of these complex trimeric structures often requires a phage-encoded tail fibre assembly (Tfa) proteins(5-7). Despite the wide occurrence of Tfa proteins, their functional mechanism has not been elucidated. Here, we investigate the tail fibre and Tfa of Escherichia coli phage Mu. We demonstrate that Tfa forms a stable complex with the tail fibre, and present a 2.1 angstrom resolution X-ray crystal structure of this complex. We find that Tfa proteins are comprised of two domains: a non-conserved N-terminal domain that binds to the C-terminal region of the fibre and a conserved C-terminal domain that probably mediates fibre oligomerization and assembly. Tfa forms rapidly exchanging multimers on its own, but not a stable trimer, implying that Tfa does not specify the trimeric state of the fibre. We propose that the key conserved role of Tfa is to ensure that fibre assembly and multimerization initiates at the C terminus, ensuring that the intertwined and repetitive structural elements of fibres come together in the correct sequence. The universal importance of correctly aligning the C termini of phage fibres is highlighted by our work.
ER  -

Basic information
Original name	Phage tail fibre assembly proteins employ a modular structure to drive the correct folding of diverse fibres
Authors	NORTH, O.I., K. SAKAI, E. YAMASHITA, A. NAKAGAWA, T. IWAZAKI, Carina Renate BÜTTNER (276 Germany, guarantor, belonging to the institution), S. TAKEDA and A.R. DAVIDSON.
Edition	Nature Microbiology, London, Nature Publishing Group, 2019, 2058-5276.

Other information
Original language	English
Type of outcome	Article in a journal
Field of Study	10606 Microbiology
Country of publisher	United Kingdom of Great Britain and Northern Ireland
Confidentiality degree	is not subject to a state or trade secret
WWW	URL
Impact factor	Impact factor: 15.540
RIV identification code	RIV/00216224:14740/19:00113245
Organization unit	Central European Institute of Technology
Doi	http://dx.doi.org/10.1038/s41564-019-0477-7
UT WoS	000487286800010
Keywords in English	EVEN-TYPE BACTERIOPHAGES; CELL-WALL RECEPTOR; HOST-RANGE; BINDING; DOMAIN; SPECIFICITY; COMPONENTS
Tags	rivok
Tags	International impact, Reviewed
Changed by	Changed by: Mgr. Pavla Foltynová, Ph.D., učo 106624. Changed: 31/3/2020 21:48.

Abstract
Phage tail fibres are elongated protein assemblies capable of specific recognition of bacterial surfaces during the first step of viral infection(1-4). The folding of these complex trimeric structures often requires a phage-encoded tail fibre assembly (Tfa) proteins(5-7). Despite the wide occurrence of Tfa proteins, their functional mechanism has not been elucidated. Here, we investigate the tail fibre and Tfa of Escherichia coli phage Mu. We demonstrate that Tfa forms a stable complex with the tail fibre, and present a 2.1 angstrom resolution X-ray crystal structure of this complex. We find that Tfa proteins are comprised of two domains: a non-conserved N-terminal domain that binds to the C-terminal region of the fibre and a conserved C-terminal domain that probably mediates fibre oligomerization and assembly. Tfa forms rapidly exchanging multimers on its own, but not a stable trimer, implying that Tfa does not specify the trimeric state of the fibre. We propose that the key conserved role of Tfa is to ensure that fibre assembly and multimerization initiates at the C terminus, ensuring that the intertwined and repetitive structural elements of fibres come together in the correct sequence. The universal importance of correctly aligning the C termini of phage fibres is highlighted by our work.

Abstract

Phage tail fibres are elongated protein assemblies capable of specific recognition of bacterial surfaces during the first step of viral infection(1-4). The folding of these complex trimeric structures often requires a phage-encoded tail fibre assembly (Tfa) proteins(5-7). Despite the wide occurrence of Tfa proteins, their functional mechanism has not been elucidated. Here, we investigate the tail fibre and Tfa of Escherichia coli phage Mu. We demonstrate that Tfa forms a stable complex with the tail fibre, and present a 2.1 angstrom resolution X-ray crystal structure of this complex. We find that Tfa proteins are comprised of two domains: a non-conserved N-terminal domain that binds to the C-terminal region of the fibre and a conserved C-terminal domain that probably mediates fibre oligomerization and assembly. Tfa forms rapidly exchanging multimers on its own, but not a stable trimer, implying that Tfa does not specify the trimeric state of the fibre. We propose that the key conserved role of Tfa is to ensure that fibre assembly and multimerization initiates at the C terminus, ensuring that the intertwined and repetitive structural elements of fibres come together in the correct sequence. The universal importance of correctly aligning the C termini of phage fibres is highlighted by our work.