Solution Structure of an Active Mutant of Maize Ribosome-Inactivating Protein (MOD) and Its Interaction with the Ribosomal Stalk Protein P2

Yang, Yinhua; Mak, Amanda Nga-Sze; Shaw, Pang‐Chui; Sze, Kong Hung

doi:10.1016/j.jmb.2009.10.051

Cited by 37 publications

(45 citation statements)

References 42 publications

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“…Previous studies examined the interaction of RIPs with individual P proteins or short peptides (33)(34)(35)(36)(37)(38), which are not found in vivo or with intact ribosomes (39,40). Here, using natively assembled stalk complexes from yeast, we show that RTA interacts directly with the yeast stalk complexes and provide the first detailed kinetic view of the interactions between RTA and the yeast ribosomal stalk.…”

Section: Kinetic Parameters Of Interaction Of Rta With Isolated Stalkmentioning

confidence: 76%

“…The individual P proteins of the ribosomal stalk or their C termini have been reported to interact with the RIPs, such as trichosanthin (33)(34)(35)(36), Stx1 (Shiga-like toxin 1) (37), and maize ribosome-inactivating protein (38). However, these studies provided only a fragmentary view of the ribosome interactions because individual P proteins or short peptides were used.…”

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confidence: 99%

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Pentameric Organization of the Ribosomal Stalk Accelerates Recruitment of Ricin A Chain to the Ribosome for Depurination

Grela

Krokowski

et al. 2010

Journal of Biological Chemistry

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Ribosome inactivating proteins (RIPs) depurinate a universally conserved adenine in the ␣-sarcin/ricin loop (SRL) and inhibit protein synthesis at the translation elongation step. We previously showed that ribosomal stalk is required for depurination of the SRL by ricin toxin A chain (RTA). The interaction between RTA and ribosomes was characterized by a twostep binding model, where the stalk structure could be considered as an important interacting element. Here, using purified yeast ribosomal stalk complexes assembled in vivo, we show a direct interaction between RTA and the isolated stalk complex. Detailed kinetic analysis of these interactions in real time using surface plasmon resonance (SPR) indicated that there is only one type of interaction between RTA and the ribosomal stalk, which represents one of the two binding steps of the interaction with ribosomes. Interactions of RTA with the isolated stalk were relatively insensitive to salt, indicating that nonelectrostatic interactions were dominant. We compared the interaction of RTA with the full pentameric stalk complex containing two pairs of P1/P2 proteins with its interaction with the trimeric stalk complexes containing only one pair of P1/P2 and found that the rate of association of RTA with the pentamer was higher than with either trimer. These results demonstrate that the stalk is the main landing platform for RTA on the ribosome and that pentameric organization of the stalk accelerates recruitment of RTA to the ribosome for depurination. Our results suggest that multiple copies of the stalk proteins might also increase the scavenging ability of the ribosome for the translational GTPases.

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Section: Kinetic Parameters Of Interaction Of Rta With Isolated Stalkmentioning

confidence: 76%

mentioning

confidence: 99%

Pentameric Organization of the Ribosomal Stalk Accelerates Recruitment of Ricin A Chain to the Ribosome for Depurination

Grela

Krokowski

et al. 2010

Journal of Biological Chemistry

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“…Each chain has a molecular weight of $30 kDa and is linked through a disulfide bond (Girbes et al, 2004). Type III RIPs consist of a single enzymatically active polypeptide, but, unlike type I RIPs, are synthesized as zymogens (Mak et al, 2007;Yang et al, 2010).…”

Section: Introductionmentioning

confidence: 99%

Structural characterization and anti-HIV-1 activities of arginine/glutamate-rich polypeptide Luffin P1 from the seeds of sponge gourd (Luffa cylindrica)

Yang

Sze

et al. 2011

Journal of Structural Biology

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Luffin P1, the smallest ribosome-inactivating peptide from the seeds of Luffa cylindrica was found to have anti-HIV-1 activity in HIV-1 infected C8166 T-cell lines and be able to bind with HIV Rev Response Element. Nuclear magnetic resonance spectroscopy revealed that the Luffin P1 comprises a helix-loop-helix motif, with the two alpha helices tightly associated by two disulfide bonds. Based on our findings, we conclude that unlike the well-studied ribosome-inactivating proteins, which exert their action through N-glycosidase activities, Luffin P1 demonstrates a novel inactivation mechanism probably through the charge complementation with viral or cellular proteins. Our work also provides a new scaffold for the design of novel inhibitors from a simple helical motif.

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“…According to this structure, the acidic amino acids at the amino end of the peptide interact with the positively charged Lys 173 , Arg 174 , and Lys 177 of TCS, whereas the hydrophobic part of the carboxyl end of the peptide is inserted into a hydrophobic pocket of TCS (33). The amino acids that interact with P2 protein are located in a different region of the maize RIP than in TCS and differ in primary sequence and electrostatic distribution (34). It has been suggested that the ability to interact with the stalk arose independently by convergent evolution (35).…”

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confidence: 99%

Arginine Residues on the Opposite Side of the Active Site Stimulate the Catalysis of Ribosome Depurination by Ricin A Chain by Interacting with the P-protein Stalk

Kahn

et al. 2013

Journal of Biological Chemistry

113

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Solution Structure of an Active Mutant of Maize Ribosome-Inactivating Protein (MOD) and Its Interaction with the Ribosomal Stalk Protein P2

Cited by 37 publications

References 42 publications

Pentameric Organization of the Ribosomal Stalk Accelerates Recruitment of Ricin A Chain to the Ribosome for Depurination

Pentameric Organization of the Ribosomal Stalk Accelerates Recruitment of Ricin A Chain to the Ribosome for Depurination

Structural characterization and anti-HIV-1 activities of arginine/glutamate-rich polypeptide Luffin P1 from the seeds of sponge gourd (Luffa cylindrica)

Arginine Residues on the Opposite Side of the Active Site Stimulate the Catalysis of Ribosome Depurination by Ricin A Chain by Interacting with the P-protein Stalk

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