Fhit proteins can also recognize substrates other than dinucleoside polyphosphates

Andrzej Guranowski; Anna M. Wojdyła; Małgorzata Pietrowska-Borek; Paweł Bieganowski; Elena N. Khurs; Matthew J. Cliff; G. Michael Blackburn; Damian Błaziak; Wojciech J. Stec

doi:10.1016/j.febslet.2008.07.060

Fhit proteins can also recognize substrates other than dinucleoside polyphosphates

Andrzej Guranowski^*, Anna M. Wojdyła, Małgorzata Pietrowska-Borek, Paweł Bieganowski, Elena N. Khurs, Matthew J. Cliff, G. Michael Blackburn, Damian Błaziak, Wojciech J. Stec

^*Corresponding author for this work

Manchester Institute of Biotechnology

Research output: Contribution to journal › Article › peer-review

Abstract

We show here that Fhit proteins, in addition to their function as dinucleoside triphosphate hydrolases, act similarly to adenylylsulfatases and nucleoside phosphoramidases, liberating nucleoside 5′-monophosphates from such natural metabolites as adenosine 5′-phosphosulfate and adenosine 5′-phosphoramidate. Moreover, Fhits recognize synthetic nucleotides, such as adenosine 5′-O-phosphorofluoridate and adenosine 5′-O-(γ-fluorotriphosphate), and release AMP from them. With respect to the former, Fhits behave like a phosphodiesterase I concomitant with cleavage of the P-F bond. Some kinetic parameters and implications of the novel reactions catalyzed by the human and plant (Arabidopsis thaliana) Fhit proteins are presented.

Original language	English
Pages (from-to)	3152-3158
Number of pages	7
Journal	FEBS Letters
Volume	582
Issue number	20
DOIs	https://doi.org/10.1016/j.febslet.2008.07.060
Publication status	Published - 3 Sept 2008

Keywords

Adenylylsulfatase activity
Dinucleoside triphosphatase activity
Fhit protein
Nucleoside phosphoramidase activity
P-F bond cleavage
Phosphodiesterase I activity

Research Beacons, Institutes and Platforms

Manchester Institute of Biotechnology

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10.1016/j.febslet.2008.07.060

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@article{289b72829ad0405793c2027bd3fbb499,

title = "Fhit proteins can also recognize substrates other than dinucleoside polyphosphates",

abstract = "We show here that Fhit proteins, in addition to their function as dinucleoside triphosphate hydrolases, act similarly to adenylylsulfatases and nucleoside phosphoramidases, liberating nucleoside 5′-monophosphates from such natural metabolites as adenosine 5′-phosphosulfate and adenosine 5′-phosphoramidate. Moreover, Fhits recognize synthetic nucleotides, such as adenosine 5′-O-phosphorofluoridate and adenosine 5′-O-(γ-fluorotriphosphate), and release AMP from them. With respect to the former, Fhits behave like a phosphodiesterase I concomitant with cleavage of the P-F bond. Some kinetic parameters and implications of the novel reactions catalyzed by the human and plant (Arabidopsis thaliana) Fhit proteins are presented.",

keywords = "Adenylylsulfatase activity, Dinucleoside triphosphatase activity, Fhit protein, Nucleoside phosphoramidase activity, P-F bond cleavage, Phosphodiesterase I activity",

author = "Andrzej Guranowski and Wojdy{\l}a, {Anna M.} and Ma{\l}gorzata Pietrowska-Borek and Pawe{\l} Bieganowski and Khurs, {Elena N.} and Cliff, {Matthew J.} and Blackburn, {G. Michael} and Damian B{\l}aziak and Stec, {Wojciech J.}",

note = "Funding Information: This work was supported by the Polish Ministry of Science and Higher Education (Grant PBZ-MNiSW-07/I/2007 to A.G., A.M.W. and M.P.-B. and Grant 2 P04A 05029 to P.B.). ",

year = "2008",

month = sep,

day = "3",

doi = "10.1016/j.febslet.2008.07.060",

language = "English",

volume = "582",

pages = "3152--3158",

journal = "FEBS Letters",

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T1 - Fhit proteins can also recognize substrates other than dinucleoside polyphosphates

AU - Guranowski, Andrzej

AU - Wojdyła, Anna M.

AU - Pietrowska-Borek, Małgorzata

AU - Bieganowski, Paweł

AU - Khurs, Elena N.

AU - Cliff, Matthew J.

AU - Blackburn, G. Michael

AU - Błaziak, Damian

AU - Stec, Wojciech J.

N1 - Funding Information: This work was supported by the Polish Ministry of Science and Higher Education (Grant PBZ-MNiSW-07/I/2007 to A.G., A.M.W. and M.P.-B. and Grant 2 P04A 05029 to P.B.).

PY - 2008/9/3

Y1 - 2008/9/3

N2 - We show here that Fhit proteins, in addition to their function as dinucleoside triphosphate hydrolases, act similarly to adenylylsulfatases and nucleoside phosphoramidases, liberating nucleoside 5′-monophosphates from such natural metabolites as adenosine 5′-phosphosulfate and adenosine 5′-phosphoramidate. Moreover, Fhits recognize synthetic nucleotides, such as adenosine 5′-O-phosphorofluoridate and adenosine 5′-O-(γ-fluorotriphosphate), and release AMP from them. With respect to the former, Fhits behave like a phosphodiesterase I concomitant with cleavage of the P-F bond. Some kinetic parameters and implications of the novel reactions catalyzed by the human and plant (Arabidopsis thaliana) Fhit proteins are presented.

AB - We show here that Fhit proteins, in addition to their function as dinucleoside triphosphate hydrolases, act similarly to adenylylsulfatases and nucleoside phosphoramidases, liberating nucleoside 5′-monophosphates from such natural metabolites as adenosine 5′-phosphosulfate and adenosine 5′-phosphoramidate. Moreover, Fhits recognize synthetic nucleotides, such as adenosine 5′-O-phosphorofluoridate and adenosine 5′-O-(γ-fluorotriphosphate), and release AMP from them. With respect to the former, Fhits behave like a phosphodiesterase I concomitant with cleavage of the P-F bond. Some kinetic parameters and implications of the novel reactions catalyzed by the human and plant (Arabidopsis thaliana) Fhit proteins are presented.

KW - Adenylylsulfatase activity

KW - Dinucleoside triphosphatase activity

KW - Fhit protein

KW - Nucleoside phosphoramidase activity

KW - P-F bond cleavage

KW - Phosphodiesterase I activity

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U2 - 10.1016/j.febslet.2008.07.060

DO - 10.1016/j.febslet.2008.07.060

M3 - Article

C2 - 18694747

AN - SCOPUS:49649089899

SN - 0014-5793

VL - 582

SP - 3152

EP - 3158

JO - FEBS Letters

JF - FEBS Letters

IS - 20

ER -

Fhit proteins can also recognize substrates other than dinucleoside polyphosphates

Abstract

Keywords

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