Literature DB >> 2960822

A eukaryotic repressor protein, the qa-1S gene product of Neurospora crassa, is homologous to part of the arom multifunctional enzyme.

I A Anton1, K Duncan, J R Coggins.   

Abstract

Little is known about the proteins involved in the control of gene expression in eukaryotes. Although some of these proteins have been sequenced, their biochemical functions are not well understood and the identification of homologies to proteins of known activities may give useful clues to the functions of these regulatory proteins. We report here that the qa-1S repressor protein of the fungus Neurospora crassa is strongly homologous to the pentafunctional arom enzyme found in many lower eukaryotes. We believe that this is the first known case of a repressor protein that is unequivocally homologous to metabolic enzymes. These findings allow us to propose likely functions for some regions of the qa-1S protein.

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Year:  1987        PMID: 2960822     DOI: 10.1016/0022-2836(87)90130-6

Source DB:  PubMed          Journal:  J Mol Biol        ISSN: 0022-2836            Impact factor:   5.469


  10 in total

1.  Differential flux through the quinate and shikimate pathways. Implications for the channelling hypothesis.

Authors:  H K Lamb; J P van den Hombergh; G H Newton; J D Moore; C F Roberts; A R Hawkins
Journal:  Biochem J       Date:  1992-05-15       Impact factor: 3.857

2.  An amino acid sequence motif observed amongst enzymes of the shikimate pathway.

Authors:  T D Bugg; P R Alefounder; C Abell
Journal:  Biochem J       Date:  1991-06-15       Impact factor: 3.857

3.  Spatial and biological characterisation of the complete quinic acid utilisation gene cluster in Aspergillus nidulans.

Authors:  H K Lamb; A R Hawkins; M Smith; I J Harvey; J Brown; G Turner; C F Roberts
Journal:  Mol Gen Genet       Date:  1990-08

4.  Identification of domains responsible for signal recognition and transduction within the QUTR transcription repressor protein.

Authors:  L J Levett; S M Si-Hoe; S Liddle; K Wheeler; D Smith; H K Lamb; G H Newton; J R Coggins; A R Hawkins
Journal:  Biochem J       Date:  2000-08-15       Impact factor: 3.857

5.  Efficient independent activity of a monomeric, monofunctional dehydroquinate synthase derived from the N-terminus of the pentafunctional AROM protein of Aspergillus nidulans.

Authors:  J D Moore; J R Coggins; R Virden; A R Hawkins
Journal:  Biochem J       Date:  1994-07-01       Impact factor: 3.857

6.  Overproduction of, and interaction within, bifunctional domains from the amino- and carboxy-termini of the pentafunctional AROM protein of Aspergillus nidulans.

Authors:  J D Moore; A R Hawkins
Journal:  Mol Gen Genet       Date:  1993-07

7.  Overproduction in Escherichia coli of the dehydroquinate synthase domain of the Aspergillus nidulans pentafunctional AROM protein.

Authors:  J P van den Hombergh; J D Moore; I G Charles; A R Hawkins
Journal:  Biochem J       Date:  1992-06-15       Impact factor: 3.857

8.  Characterization of the 3-dehydroquinase domain of the pentafunctional AROM protein, and the quinate dehydrogenase from Aspergillus nidulans, and the overproduction of the type II 3-dehydroquinase from neurospora crassa.

Authors:  A R Hawkins; J D Moore; A M Adeokun
Journal:  Biochem J       Date:  1993-12-01       Impact factor: 3.857

9.  Molecular organisation of the quinic acid utilization (QUT) gene cluster in Aspergillus nidulans.

Authors:  A R Hawkins; H K Lamb; M Smith; J W Keyte; C F Roberts
Journal:  Mol Gen Genet       Date:  1988-10

10.  Comparative analysis of the QUTR transcription repressor protein and the three C-terminal domains of the pentafunctional AROM enzyme.

Authors:  H K Lamb; J D Moore; J H Lakey; L J Levett; K A Wheeler; H Lago; J R Coggins; A R Hawkins
Journal:  Biochem J       Date:  1996-02-01       Impact factor: 3.857

  10 in total

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