共查询到3条相似文献,搜索用时 0 毫秒
1.
Proteins interacting with the biological information molecules DNA and RNA play important cellular roles in all organisms.
One widespread super family of proteins implicated in such function(s) is cold shock protein (CSP) that contains the cold
shock domain (CSD). This work is planned to study the three-dimensional structure, conserved residues, and different active
sites in the structure of cold resistant protein (CRP) from CRPF1, cold tolerant mutant of Pseudomonas fluorescence by comparative homology modeling. Here we tried to identify crucial residues that are involved in active sites or functional
sites of the protein. The study reveals that CRP represent the prototype of the CSD and share a highly similar overall fold
consisting of five antiparallel β-sheets forming a β-barrel structure with surface exposed aromatic and basic residues that
were responsible for nucleic acid binding properties of variable binding affinities and sequence selectivity and harbors the
nucleic acid binding motifs RNP1 and RNP2 that is highly conserved in CSP family. 相似文献
2.
Kun Wang Feng Gao Renshan Zhu Shaoqing Li Yingguo Zhu 《Plant Molecular Biology Reporter》2011,29(3):739-744
Pentatricopeptide repeat protein (PPR) proteins are putative RNA-binding proteins which are particularly prevalent in terrestrial
plants. Previous research has reported the great difficulty in purifying soluble PPR proteins in Escherichia coli, therefore hindering further study of their functions. In this paper, we report the use of the pMAL
™
prokaryotic expression system to acquire a soluble expression of a PPR protein, RF1A from rice (Oryza sativa L.). After purification, we identified RF1A by ESI-TOF-MS/MS. We also made an estimation of its secondary structure using
the circular dichroism spectroscopy. These results supported the bioinformatic prediction of helical-hairpin model about PPR
proteins. 相似文献
3.
Priscila Camillo Teixeira Leonardo Garcia Velasquez Ana Paula Lepique Eloiza de Rezende José Matheus Camargo Bonatto Marcello Andre Barcinski Edecio Cunha-Neto Beatriz Simonsen Stolf 《PLoS neglected tropical diseases》2015,9(2)
Leishmaniasis is an important disease that affects 12 million people in 88 countries, with 2 million new cases every year. Leishmania amazonensis is an important agent in Brazil, leading to clinical forms varying from localized (LCL) to diffuse cutaneous leishmaniasis (DCL). One interesting issue rarely analyzed is how host immune response affects Leishmania phenotype and virulence. Aiming to study the effect of host immune system on Leishmania proteins we compared proteomes of amastigotes isolated from BALB/c and BALB/c nude mice. The athymic nude mice may resemble patients with diffuse cutaneous leishmaniasis, considered T-cell hyposensitive or anergic to Leishmania´s antigens. This work is the first to compare modifications in amastigotes’ proteomes driven by host immune response. Among the 44 differentially expressed spots, there were proteins related to oxidative/nitrosative stress and proteases. Some correspond to known Leishmania virulence factors such as OPB and tryparedoxin peroxidase. Specific isoforms of these two proteins were increased in parasites from nude mice, suggesting that T cells probably restrain their posttranslational modifications in BALB/c mice. On the other hand, an isoform of HSP70 was increased in amastigotes from BALB/c mice. We believe our study may allow identification of potential virulence factors and ways of regulating their expression. 相似文献