The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

Links

 

Gene Review

NIP1  -  Nip1p

Saccharomyces cerevisiae S288c

Synonyms: Eukaryotic translation initiation factor 3 93 kDa subunit, Eukaryotic translation initiation factor 3 subunit C, Nuclear transport protein NIP1, Translation initiation factor eIF3, p93 subunit, YM9924.01C, ...
 
 
Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.
 

High impact information on NIP1

  • The TIF32-CTD interacted in vitro with helices 16-18 of domain I in 18S rRNA, and the TIF32-NTD and NIP1 interacted with 40S protein RPS0A [1].
  • The yeast eIF3 subunits TIF32/a, NIP1/c, and eIF5 make critical connections with the 40S ribosome in vivo [1].
  • In addition to the contact between eIF2 and the N-terminal domain (NTD) of NIP1 bridged by eIF5, the C-terminal domain (CTD) of TIF32 binds eIF2 directly and is required for eIF2-eIF3 association in vivo [2].
  • Thus, several key functions of eIF3 can be carried out by the PRT1-TIF32-NIP1 subcomplex [3].
  • NIP1, a gene required for nuclear transport in yeast [4].
 

Biological context of NIP1

  • NIP1+ was shown to be an essential gene by gene disruption experiments [4].
  • Both effects of this NIP1 mutation were suppressed by eIF1 overexpression, as was the Sui(-) phenotype conferred by eIF5-G31R [5].
  • Analysis of the cloned cDNA encoding p110 indicates that its amino acid sequence is 31% identical to that of the yeast protein, Nip1 [6].
 

Associations of NIP1 with chemical compounds

  • Furthermore, an epitope-labeled NIP1 protein migrated in SDS/polyacrylamide gels with a mass of approximately 100,000 Da and was shown by immunofluorescence to localize mainly in the cytoplasm [4].
 

Physical interactions of NIP1

  • The N-terminal domain (NTD) of NIP1/eIF3c interacts directly with eIF1 and eIF5 and indirectly through eIF5 with the eIF2-GTP-Met-tRNA(i)(Met) ternary complex (TC) to form the multifactor complex (MFC) [5].
 

Other interactions of NIP1

  • His8-PRT1 and NIP1 did not form a stable binary subcomplex [3].

References

  1. The yeast eIF3 subunits TIF32/a, NIP1/c, and eIF5 make critical connections with the 40S ribosome in vivo. Valásek, L., Mathew, A.A., Shin, B.S., Nielsen, K.H., Szamecz, B., Hinnebusch, A.G. Genes Dev. (2003) [Pubmed]
  2. Direct eIF2-eIF3 contact in the multifactor complex is important for translation initiation in vivo. Valásek, L., Nielsen, K.H., Hinnebusch, A.G. EMBO J. (2002) [Pubmed]
  3. A subcomplex of three eIF3 subunits binds eIF1 and eIF5 and stimulates ribosome binding of mRNA and tRNA(i)Met. Phan, L., Schoenfeld, L.W., Valásek, L., Nielsen, K.H., Hinnebusch, A.G. EMBO J. (2001) [Pubmed]
  4. NIP1, a gene required for nuclear transport in yeast. Gu, Z., Moerschell, R.P., Sherman, F., Goldfarb, D.S. Proc. Natl. Acad. Sci. U.S.A. (1992) [Pubmed]
  5. Interactions of eukaryotic translation initiation factor 3 (eIF3) subunit NIP1/c with eIF1 and eIF5 promote preinitiation complex assembly and regulate start codon selection. Valásek, L., Nielsen, K.H., Zhang, F., Fekete, C.A., Hinnebusch, A.G. Mol. Cell. Biol. (2004) [Pubmed]
  6. Conservation and diversity of eukaryotic translation initiation factor eIF3. Asano, K., Kinzy, T.G., Merrick, W.C., Hershey, J.W. J. Biol. Chem. (1997) [Pubmed]
 
WikiGenes - Universities