Biomedical subjects

Mengwen Jia

Publications and source records attributed to Mengwen Jia.

4 recordsLinked to original sources

PubMed2006

The relation between mRNA folding and protein structure.

About 200 mRNA sequences of Escherichia coli and human with matching protein secondary structure data were studied. The mRNA folding for each native sequence and for corresponding randomized sequences was calculated through free energy minimization. We have found that the folding energy of mRNA segments in different protein secondary structures is significantly different. The average Z score is more negative for regular secondary structure (alpha-helix and beta-strand) than that for coil. This suggests that the codon choice in native mRNA sequence coding for protein regular structure contributes more to the mRNA folding stability.

Escherichia coli Proteins↗

PubMed2005

The relationship among gene expression, folding free energy and codon usage bias in Escherichia coli.

Taking advantage of microarray data in Escherichia coli genome, the relationship among mRNA expression levels, folding free energy and codon usage bias are investigated. Our results indicate that mRNA expression is correlated to the stability of mRNA secondary structure and the codon usage bias. The decrease of the stability of mRNA structure contributes to the increase of mRNA expression. There is a negative correlation between codon adaptation index (CAI) and mRNA expression in genes with less stable structure. The relationship between the stability of mRNA structure and mRNA half-life indicates the stability of mRNA structure is different from mRNA half-life.

Codon↗

PubMed2004

Protein structure preference, tRNA copy number, and mRNA stem/loop content.

From statistical analyses of protein sequences for humans and Escherichia coli we found that the messenger RNA segment of m-codons (for m=2 to 6) with average high tRNA copy number (TCN) (larger than approximately 10.5 for humans or approximately 1.95 for E. coli) preferably code for the alpha helix and that with low TCN (smaller than approximately 7.5 for humans or approximately 1.7 for E. coli) preferably code for coil. Between them there is an intermediate region without correlation to structure preference. For the beta strand the preference/ avoidance tendency is not obvious. All strong preference-modes of TCN for protein secondary structures have been deduced. The mutual interaction between two factors--protein secondary structural type and codon TCN--is tested by F distribution. A phenomenological model on the relation between structure preference and translational efficiency or accuracy is proposed. It is pointed out that the structure preference of codons is related to the distribution of mRNA stem/loop content in three TCN regions.

Bacterial Proteins↗

PubMed2004

Statistical correlation between protein secondary structure and messenger RNA stem-loop structure.

A new integrated sequence-structure database, called IADE (Integrated ASTRAL-DSSP-EMBL), incorporating matching mRNA sequence, amino acid sequence, and protein secondary structural data, is constructed. It includes 648 protein domains. Based on the IADE database, we studied the relation between RNA stem-loop frequencies and protein secondary structure. It was found that the alpha-helices and beta-strands on proteins tend to be preferably "coded" by mRNA stem region, while the coils on proteins tend to be preferably "coded" by mRNA loop region. These tendencies are more obvious if we observe the structural words (SWs). An SW is defined by a four-amino-acid-fragment that shows the pronounced secondary structural (alpha-helix or beta-strand) propensity. It is demonstrated that the deduced correlation between protein and mRNA structure can hardly be explained as the stochastic fluctuation effect.

Databases as Topic↗