Introduction: Difference between revisions

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Gene expression is highly regulated by complex protein translation systems. Expression within the eukaryotic cell is especially complicated, involving the mature mRNA, the ribosomal subunits and other protein factors. Furthermore, each component has to interact in a specific function i.e. the small ribosomal subunit has to recognise a start codon, and the large ribosomal subunit has to be recruited before translation can be initiated (Wagner et al.''YEAR''). One such protein is the eukaryotic translation initiation factor 4G (eIF4G), which participates in the recruiting of the small 40S ribosomal subunit and in scanning along the 5' UTR of the mRNA to the translation start codon. Other regulatory proteins which interact in tandem with the eIF4G include the 5'-cap-binding protein eIF4E and RNA helicase eIF4A.
=='''Introduction''' ==


An MIF4G-like protein from the zebrafish was studied for its functional, structural and evolutionary properties. Preliminary information provided by the crystal structure of the protein revealed it to be similar to the middle domain of the eIF4G protein, hence described as "MIF4G-like protein". Subsequent research into the MIF4G protein is presented in this report.


 
Nucleotide binding protein 2 is a novel protein defined which represent the eukaryotic nucleotide binding protein family. NUBP2 represent the short form of nucleotide binding protein which  belongs to the partitioning ATPase gene family. The protein from this family function by drawing energy from hydrolysis of ATP, and they share a characteristic sequence motif of “[GA]-X2-(G)-X-G-K-[ST],” called the “phosphate-binding loop (P-loop)” (Walker et al., 1982; Saraste et al., 1990). Although the structure of NUBP2 is not completely solved, but the high similarity of NUBP2 with 2ph1 (MinD homologue, E.coli) make the function analysis possible.  
**I think we should have some information here about the eIF domain. Ie that is consists of x number of domains of which MIF4G is the middle domain. etc. Maybe some information on what this does (although we mostly have that anyway). I will do something on this and add it. if thats ok with everyone - if not let me know. :)
E.coli MinD was also included in the Partitioning ATPase gene family, it is a membrane associated ATPase which inhibits the cell division at the poles and consequently induces normal cell division (de Boer et al., 1991), and based on sequence similarity, the E. coli mrp gene (Dardel et al., 1990). The similarity between 2ph1 and NUBP2 is about 39.66% of the sequence, and by using the structure of 2ph1, the function of NUBP2 would be analysed based on the structure searching.
 
The division septum is normally placed at the midpoint of the cell, but potential division sites also exist near each of the cell poles. Restriction of the cell division site at the midpoint is governed by the product of the three genes of the MinB operon, MinC, MinD and MinE. MinC inhibits the division at all of the potential division sites and requires the activity of peripheral membrane ATPase MinD for its function. MinC and MinD act cooperatively to form a non-specific division inhibitor complex. MinE has two functions: it suppresses the MinCD-mediated division inhibition and recognizes the mid-cell point from the cell poles. In order words, MinE promotes mid-cell division by excluding MinCD from the mid-cell site.
 
Based on the homology similarity of NUBP2 to E. coli MinD protein, we hypothesed that NUBP2 involves in cell division to determine the position of septum (Z-ring). Another function of this protein is hydrolyse ATP molecules in cell. Further analysis was conducted in structural study on NUBP2 to deduce the function of NUBP2 protein.
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Latest revision as of 07:40, 2 June 2009

Introduction

Nucleotide binding protein 2 is a novel protein defined which represent the eukaryotic nucleotide binding protein family. NUBP2 represent the short form of nucleotide binding protein which belongs to the partitioning ATPase gene family. The protein from this family function by drawing energy from hydrolysis of ATP, and they share a characteristic sequence motif of “[GA]-X2-(G)-X-G-K-[ST],” called the “phosphate-binding loop (P-loop)” (Walker et al., 1982; Saraste et al., 1990). Although the structure of NUBP2 is not completely solved, but the high similarity of NUBP2 with 2ph1 (MinD homologue, E.coli) make the function analysis possible. E.coli MinD was also included in the Partitioning ATPase gene family, it is a membrane associated ATPase which inhibits the cell division at the poles and consequently induces normal cell division (de Boer et al., 1991), and based on sequence similarity, the E. coli mrp gene (Dardel et al., 1990). The similarity between 2ph1 and NUBP2 is about 39.66% of the sequence, and by using the structure of 2ph1, the function of NUBP2 would be analysed based on the structure searching. The division septum is normally placed at the midpoint of the cell, but potential division sites also exist near each of the cell poles. Restriction of the cell division site at the midpoint is governed by the product of the three genes of the MinB operon, MinC, MinD and MinE. MinC inhibits the division at all of the potential division sites and requires the activity of peripheral membrane ATPase MinD for its function. MinC and MinD act cooperatively to form a non-specific division inhibitor complex. MinE has two functions: it suppresses the MinCD-mediated division inhibition and recognizes the mid-cell point from the cell poles. In order words, MinE promotes mid-cell division by excluding MinCD from the mid-cell site. Based on the homology similarity of NUBP2 to E. coli MinD protein, we hypothesed that NUBP2 involves in cell division to determine the position of septum (Z-ring). Another function of this protein is hydrolyse ATP molecules in cell. Further analysis was conducted in structural study on NUBP2 to deduce the function of NUBP2 protein.

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