Literature DB >> 1314899

NAM7 nuclear gene encodes a novel member of a family of helicases with a Zn-ligand motif and is involved in mitochondrial functions in Saccharomyces cerevisiae.

N Altamura1, O Groudinsky, G Dujardin, P P Slonimski.   

Abstract

The yeast nuclear gene NAM7 was previously isolated within a genomic fragment of 7.7 kb (1 kb = 10(3) bases or base-pairs), having the ability to suppress mitochondrial intronic mutations defective in RNA splicing. We have identified and sequenced the region on the insert corresponding to the NAM7 gene. A long open reading frame has been revealed which could code for a protein of 971 amino acids. Comparison of the NAM7 putative protein with data libraries did not reveal any strong similarity with known proteins. However, the NAM7 protein contains several motifs typical for proteins interacting with nucleic acids: (1) five motifs diagnostic for a superfamily of helicases appear in the same order and with similar distances; (2) the N-terminal portion possesses potential Zn-ligand structures belonging to the C chi superfamily. Deletion of the chromosomal copy of NAM7 gene leads to a partial impairment in respiratory growth that is particularly striking at low temperature. Southern blot analysis of DNA extracted from a nam7 :: URA3 deleted strain revealed the presence of a second gene whose sequence is related to that of the NAM7 gene and which could participate in the same process.

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Year:  1992        PMID: 1314899     DOI: 10.1016/0022-2836(92)90545-u

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


  42 in total

1.  Comparative genomics and evolution of proteins involved in RNA metabolism.

Authors:  Vivek Anantharaman; Eugene V Koonin; L Aravind
Journal:  Nucleic Acids Res       Date:  2002-04-01       Impact factor: 16.971

2.  Mtt1 is a Upf1-like helicase that interacts with the translation termination factors and whose overexpression can modulate termination efficiency.

Authors:  K Czaplinski; N Majlesi; T Banerjee; S W Peltz
Journal:  RNA       Date:  2000-05       Impact factor: 4.942

Review 3.  NMD mechanism and the functions of Upf proteins in plant.

Authors:  Yiming Dai; Wenli Li; Lijia An
Journal:  Plant Cell Rep       Date:  2015-09-23       Impact factor: 4.570

4.  A yeast gene required for DNA replication encodes a protein with homology to DNA helicases.

Authors:  M E Budd; J L Campbell
Journal:  Proc Natl Acad Sci U S A       Date:  1995-08-15       Impact factor: 11.205

5.  The majority of yeast UPF1 co-localizes with polyribosomes in the cytoplasm.

Authors:  A L Atkin; N Altamura; P Leeds; M R Culbertson
Journal:  Mol Biol Cell       Date:  1995-05       Impact factor: 4.138

6.  Identification and characterization of mutations in the UPF1 gene that affect nonsense suppression and the formation of the Upf protein complex but not mRNA turnover.

Authors:  Y Weng; K Czaplinski; S W Peltz
Journal:  Mol Cell Biol       Date:  1996-10       Impact factor: 4.272

7.  Genetic and biochemical characterization of mutations in the ATPase and helicase regions of the Upf1 protein.

Authors:  Y Weng; K Czaplinski; S W Peltz
Journal:  Mol Cell Biol       Date:  1996-10       Impact factor: 4.272

8.  The surveillance complex interacts with the translation release factors to enhance termination and degrade aberrant mRNAs.

Authors:  K Czaplinski; M J Ruiz-Echevarria; S V Paushkin; X Han; Y Weng; H A Perlick; H C Dietz; M D Ter-Avanesyan; S W Peltz
Journal:  Genes Dev       Date:  1998-06-01       Impact factor: 11.361

9.  A mutated human homologue to yeast Upf1 protein has a dominant-negative effect on the decay of nonsense-containing mRNAs in mammalian cells.

Authors:  X Sun; H A Perlick; H C Dietz; L E Maquat
Journal:  Proc Natl Acad Sci U S A       Date:  1998-08-18       Impact factor: 11.205

10.  THRAP3 interacts with HELZ2 and plays a novel role in adipocyte differentiation.

Authors:  Akiko Katano-Toki; Tetsurou Satoh; Takuya Tomaru; Satoshi Yoshino; Takahiro Ishizuka; Sumiyasu Ishii; Atsushi Ozawa; Nobuyuki Shibusawa; Takafumi Tsuchiya; Tsugumichi Saito; Hiroyuki Shimizu; Koshi Hashimoto; Shuichi Okada; Masanobu Yamada; Masatomo Mori
Journal:  Mol Endocrinol       Date:  2013-03-22
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