Literature DB >> 9188639

Identification of an ATPase activity associated with a 71-kilodalton polypeptide encoded in gene 1 of the human coronavirus 229E.

G Heusipp1, U Harms, S G Siddell, J Ziebuhr.   

Abstract

Human coronavirus 229E gene expression involves proteolytic processing of the gene 1-encoded polyproteins pp1a and pp1ab. In this study, we have detected a 71-kDa polypeptide in virus-infected cells that is released from pp1ab by the virus-encoded 3C-like proteinase and that has been predicted to contain both metal-binding and helicase domains. The polypeptide encompasses amino acids Ala-4996 to Gln-5592 of pp1ab and exhibits nucleic acid-stimulated ATPase activity when expressed as a fusion protein with the Escherichia coli maltose-binding protein. These data provide the first identification of a coronavirus open reading frame 1b-encoded enzymatic activity.

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Year:  1997        PMID: 9188639      PMCID: PMC191807          DOI: 10.1128/JVI.71.7.5631-5634.1997

Source DB:  PubMed          Journal:  J Virol        ISSN: 0022-538X            Impact factor:   5.103


  30 in total

1.  ATPase, GTPase, and RNA binding activities associated with the 206-kilodalton protein of turnip yellow mosaic virus.

Authors:  G Kadaré; C David; A L Haenni
Journal:  J Virol       Date:  1996-11       Impact factor: 5.103

2.  Expression and characterization of a recombinant murine coronavirus 3C-like proteinase.

Authors:  A Seybert; J Ziebuhr; S G Siddell
Journal:  J Gen Virol       Date:  1997-01       Impact factor: 3.891

3.  Characterization of coronavirus RNA polymerase gene products.

Authors:  J Herold; S Siddell; J Ziebuhr
Journal:  Methods Enzymol       Date:  1996       Impact factor: 1.600

4.  RNA helicase activity associated with the human p68 protein.

Authors:  H Hirling; M Scheffner; T Restle; H Stahl
Journal:  Nature       Date:  1989-06-15       Impact factor: 49.962

5.  Intracellular and in vitro-translated 27-kDa proteins contain the 3C-like proteinase activity of the coronavirus MHV-A59.

Authors:  X Lu; Y Lu; M R Denison
Journal:  Virology       Date:  1996-08-15       Impact factor: 3.616

6.  Biosynthesis, purification, and characterization of the human coronavirus 229E 3C-like proteinase.

Authors:  J Ziebuhr; G Heusipp; S G Siddell
Journal:  J Virol       Date:  1997-05       Impact factor: 5.103

7.  Characterisation and mutational analysis of an ORF 1a-encoding proteinase domain responsible for proteolytic processing of the infectious bronchitis virus 1a/1b polyprotein.

Authors:  D X Liu; T D Brown
Journal:  Virology       Date:  1995-06-01       Impact factor: 3.616

Review 8.  A novel superfamily of nucleoside triphosphate-binding motif containing proteins which are probably involved in duplex unwinding in DNA and RNA replication and recombination.

Authors:  A E Gorbalenya; E V Koonin; A P Donchenko; V M Blinov
Journal:  FEBS Lett       Date:  1988-08-01       Impact factor: 4.124

9.  Characterization of a 105-kDa polypeptide encoded in gene 1 of the human coronavirus HCV 229E.

Authors:  C Grötzinger; G Heusipp; J Ziebuhr; U Harms; J Süss; S G Siddell
Journal:  Virology       Date:  1996-08-01       Impact factor: 3.616

10.  Coronavirus genome: prediction of putative functional domains in the non-structural polyprotein by comparative amino acid sequence analysis.

Authors:  A E Gorbalenya; E V Koonin; A P Donchenko; V M Blinov
Journal:  Nucleic Acids Res       Date:  1989-06-26       Impact factor: 16.971

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  26 in total

1.  The human coronavirus 229E superfamily 1 helicase has RNA and DNA duplex-unwinding activities with 5'-to-3' polarity.

Authors:  A Seybert; A Hegyi; S G Siddell; J Ziebuhr
Journal:  RNA       Date:  2000-07       Impact factor: 4.942

2.  Membrane association and dimerization of a cysteine-rich, 16-kilodalton polypeptide released from the C-terminal region of the coronavirus infectious bronchitis virus 1a polyprotein.

Authors:  Lisa F P Ng; D X Liu
Journal:  J Virol       Date:  2002-06       Impact factor: 5.103

3.  Biochemical characterization of the equine arteritis virus helicase suggests a close functional relationship between arterivirus and coronavirus helicases.

Authors:  A Seybert; L C van Dinten; E J Snijder; J Ziebuhr
Journal:  J Virol       Date:  2000-10       Impact factor: 5.103

4.  Four proteins processed from the replicase gene polyprotein of mouse hepatitis virus colocalize in the cell periphery and adjacent to sites of virion assembly.

Authors:  A G Bost; R H Carnahan; X T Lu; M R Denison
Journal:  J Virol       Date:  2000-04       Impact factor: 5.103

5.  A complex zinc finger controls the enzymatic activities of nidovirus helicases.

Authors:  Anja Seybert; Clara C Posthuma; Leonie C van Dinten; Eric J Snijder; Alexander E Gorbalenya; John Ziebuhr
Journal:  J Virol       Date:  2005-01       Impact factor: 5.103

6.  Processing of the human coronavirus 229E replicase polyproteins by the virus-encoded 3C-like proteinase: identification of proteolytic products and cleavage sites common to pp1a and pp1ab.

Authors:  J Ziebuhr; S G Siddell
Journal:  J Virol       Date:  1999-01       Impact factor: 5.103

7.  Identification of a 24-kDa polypeptide processed from the coronavirus infectious bronchitis virus 1a polyprotein by the 3C-like proteinase and determination of its cleavage sites.

Authors:  L F Ng; D X Liu
Journal:  Virology       Date:  1998-04-10       Impact factor: 3.616

8.  ADP-ribose-1"-monophosphatase: a conserved coronavirus enzyme that is dispensable for viral replication in tissue culture.

Authors:  Akos Putics; Witold Filipowicz; Jonathan Hall; Alexander E Gorbalenya; John Ziebuhr
Journal:  J Virol       Date:  2005-10       Impact factor: 5.103

9.  Further identification and characterization of novel intermediate and mature cleavage products released from the ORF 1b region of the avian coronavirus infectious bronchitis virus 1a/1b polyprotein.

Authors:  H Y Xu; K P Lim; S Shen; D X Liu
Journal:  Virology       Date:  2001-09-30       Impact factor: 3.616

10.  Proteolytic processing of the open reading frame 1b-encoded part of arterivirus replicase is mediated by nsp4 serine protease and Is essential for virus replication.

Authors:  L C van Dinten; S Rensen; A E Gorbalenya; E J Snijder
Journal:  J Virol       Date:  1999-03       Impact factor: 5.103

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