Ubiquitination of mRNA cycling sequence binding protein from Leishmania donovani (LdCSBP) modulates the RNA endonuclease activity of its Smr domain

FEBS Letters ◽  
2011 ◽  
Vol 585 (5) ◽  
pp. 809-813 ◽  
Author(s):  
Dipankar Bhandari ◽  
Kasturi Guha ◽  
Nipa Bhaduri ◽  
Partha Saha
2017 ◽  
Vol 114 (8) ◽  
pp. E1554-E1563 ◽  
Author(s):  
Wen Zhou ◽  
Qingtao Lu ◽  
Qingwei Li ◽  
Lei Wang ◽  
Shunhua Ding ◽  
...  

Numerous attempts have been made to identify and engineer sequence-specific RNA endonucleases, as these would allow for efficient RNA manipulation. However, no natural RNA endonuclease that recognizes RNA in a sequence-specific manner has been described to date. Here, we report that SUPPRESSOR OF THYLAKOID FORMATION 1 (SOT1), anArabidopsispentatricopeptide repeat (PPR) protein with a small MutS-related (SMR) domain, has RNA endonuclease activity. We show that the SMR moiety of SOT1 performs the endonucleolytic maturation of 23S and 4.5S rRNA through the PPR domain, specifically recognizing a 13-nucleotide RNA sequence in the 5′ end of the chloroplast 23S–4.5S rRNA precursor. In addition, we successfully engineered the SOT1 protein with altered PPR motifs to recognize and cleave a predicted RNA substrate. Our findings point to SOT1 as an exciting tool for RNA manipulation.


1999 ◽  
Vol 337 (3) ◽  
pp. 551-558 ◽  
Author(s):  
Abhijit GHOSH ◽  
Keya BANDYOPADHYAY ◽  
Labanyamoy KOLE ◽  
Pijush K. DAS

Extracellular matrix (ECM)-binding proteins on the surface of Leishmania are thought to play a crucial role in the onset of leishmaniasis, as these parasites invade mononuclear phagocytes in various organs after migrating through the ECM. In a previous report, we presented several lines of evidence suggesting that Leishmania has a specific receptor for laminin, a major ECM protein, with a Kd in the nanomolar range. Here we describe the identification, purification and biochemical characterization of the Leishmania laminin receptor. When the outer membrane proteins of L. donovani were blotted on to nitrocellulose paper and probed with laminin, a prominent laminin-binding protein of 67 kDa was identified. The purified protein was isolated by a three-step process involving DEAE–cellulose, Con A (concanavalin A)–Sepharose and laminin–Sepharose affinity chromatography and was used to raise a monospecific antibody. The same protein was obtained when parasite membrane extracts were adsorbed to antibody affinity matrix and eluted with glycine. The affinity-purified protein bound to laminin in a detergent-solubilized form as well as after integration into artificial bilayers, and was subsequently characterized as an integral membrane protein. Metaperiodate oxidation and metabolic inhibition of glycosylation studies indicate the binding protein to be glycoprotein in nature and that N-linked oligosaccharides play a part in the interaction of laminin with the binding protein. Surface-labelled parasites attached to microtitre wells coated with laminin and the 67 kDa protein blocked the adhesion to laminin substrate. We propose that the 67 kDa protein is an adhesin involved in the attachment of Leishmaniato host tissues.


Biochimie ◽  
2015 ◽  
Vol 115 ◽  
pp. 120-135 ◽  
Author(s):  
Amir Zaidi ◽  
Krishn Pratap Singh ◽  
Shadab Anwar ◽  
Shashi S. Suman ◽  
Asif Equbal ◽  
...  

2012 ◽  
Vol 84 (5) ◽  
pp. 2492-2497 ◽  
Author(s):  
Nana Yang ◽  
Ya Cao ◽  
Ping Han ◽  
Xuejun Zhu ◽  
Lizhou Sun ◽  
...  

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