scholarly journals Roles of the Tetratricopeptide Repeat Domain inO-GlcNAc Transferase Targeting and Protein Substrate Specificity

2003 ◽  
Vol 278 (27) ◽  
pp. 24608-24616 ◽  
Author(s):  
Sai Prasad N. Iyer ◽  
Gerald W. Hart
Keyword(s):  
Substrate Specificity ◽  
Tetratricopeptide Repeat ◽  
Protein Substrate ◽  
Repeat Domain ◽  
Tetratricopeptide Repeat Domain ◽  
Glcnac Transferase

scholarly journals Protein substrates engage the lumen of O-GlcNac transferase’s tetratricopeptide repeat domain in different ways

2020 ◽  
Author(s):  
Cassandra M. Joiner ◽  
Forrest A. Hammel ◽  
John Janetzko ◽  
Suzanne Walker
Keyword(s):  
Tetratricopeptide Repeat ◽  
Substrate Selection ◽  
Post Translational Modification ◽  
Protein Substrates ◽  
Cytoplasmic Proteins ◽  
C Terminus ◽  
Glycosylation Sites ◽  
Repeat Domain ◽  
Tetratricopeptide Repeat Domain ◽  
Glcnac Transferase

ABSTRACTGlycosylation of nuclear and cytoplasmic proteins is an essential post-translational modification in mammals. O-GlcNAc transferase (OGT), the sole enzyme responsible for this modification, glycosylates over a thousand unique nuclear and cytoplasmic substrates. How OGT selects its substrates is a fundamental question that must be answered to understand OGT’s unusual biology. OGT contains a long tetratricopeptide repeat (TPR) domain that has been implicated in substrate selection, but there is almost no information about how changes to this domain affect glycosylation of individual substrates. Here, we used proteome-wide glycosylation profiling and probed glycosylation of selected purified substrates to show that asparagine and aspartate ladders that extend the full length of OGT’s TPR lumen control substrate glycosylation. We also found that substrates with glycosylation sites close to the C-terminus bypass lumenal binding. Our findings demonstrate that substrates can engage OGT in a variety of different ways for glycosylation.

scholarly journals REASSESSMENT OF THE CATALYTIC ACTIVITY AND SUBSTRATE SPECIFICITY OF FKBP35 FROM Plasmodium knowlesi USING PROTEASE-FREE ASSAY

2020 ◽  
pp. 125
Author(s):  
Cahyo Budiman ◽  
Carlmond Goh Kah Wun ◽  
Lee Ping Chin ◽  
Rafida Razali ◽  
Thean Chor Leow
Keyword(s):  
Catalytic Activity ◽  
Substrate Specificity ◽  
Catalytic Domain ◽  
Plasmodium Knowlesi ◽  
Tetratricopeptide Repeat ◽  
Cleavage Sites ◽  
Repeat Domain ◽  
The Common ◽  
Tetratricopeptide Repeat Domain ◽  
Promising Avenue

FK506-binding protein35 of Plasmodium knowlesi (Pk-FKBP35) is a member of peptidyl prolyl cis-trans isomerase (PPIase) and is considered as a promising avenue of antimalarial drug target development. This protein is organized into the N-terminal domain responsible for PPIase catalytic activity followed and the tetratricopeptide repeat domain for its dimerization. The protease-coupling and protease-free assays are known to be the common methods for investigating the catalytic properties of PPIase. Earlier, the protease-coupling assay was used to confirm the catalytic activity of Pk-FKBP35 in accelerating cis-trans isomerization of the peptide substrate. This report is aimed to re-assess the catalytic and substrate specificity of Pk-FKBP35 using an alternative method of a protease-free assay. The result indicated that while Pk-FKBP35 theoretically contained many possible cleavage sites of chymotrypsin, experimentally, the catalytic domain was relatively stable from chymotrypsin. Furthermore, under protease-free assay, Pk-FKBP35 also demonstrated remarkable PPIase catalytic activity with kcat/KM of 4.5 + 0.13 × 105 M−1 s−1, while the kcat/KM of active site mutant of D55A is 0.81 + 0.05 × 105 M−1 s−1. These values were considered comparable to kcat/KM obtained from the protease-coupling assay. Interestingly, the substrate specificities of Pk-FKBP35 obtained from both methods are also similar, with the preference of Pk-FKBP35 towards Xaa at P1 position was Leu>Phe>Lys>Trp>Val>Ile>His>Asp>Ala>Gln>Glu. Altogether, we proposed that protease-free and protease-coupling assays arereliable for Pk-FKBP35.

scholarly journals C-terminal Sequences outside the Tetratricopeptide Repeat Domain of FKBP51 and FKBP52 Cause Differential Binding to Hsp90

2003 ◽  
Vol 278 (19) ◽  
pp. 17388-17394 ◽  
Author(s):  
Joyce Cheung-Flynn ◽  
Patricia J. Roberts ◽  
Daniel L. Riggs ◽  
David F. Smith
Keyword(s):  
Tetratricopeptide Repeat ◽  
Repeat Domain ◽  
Differential Binding ◽  
Tetratricopeptide Repeat Domain

scholarly journals Hybrid Sterility in Rice (Oryza sativaL.) Involves the Tetratricopeptide Repeat Domain Containing Protein

Genetics ◽  
2016 ◽  
Vol 203 (3) ◽  
pp. 1439-1451 ◽  
Author(s):  
Yang Yu ◽  
Zhigang Zhao ◽  
Yanrong Shi ◽  
Hua Tian ◽  
Linglong Liu ◽  
...  
Keyword(s):  
Hybrid Sterility ◽  
Tetratricopeptide Repeat ◽  
Repeat Domain ◽  
Tetratricopeptide Repeat Domain

Biallelic Mutations in Tetratricopeptide Repeat Domain 26 ( Intraflagellar Transport 56 ) Cause Severe Biliary Ciliopathy in Humans

Hepatology ◽  
2020 ◽  
Vol 71 (6) ◽  
pp. 2067-2079 ◽  
Author(s):  
Ranad Shaheen ◽  
Saud Alsahli ◽  
Nour Ewida ◽  
Fatema Alzahrani ◽  
Hanan E. Shamseldin ◽  
...  
Keyword(s):  
Intraflagellar Transport ◽  
Tetratricopeptide Repeat ◽  
Repeat Domain ◽  
Tetratricopeptide Repeat Domain ◽  
Biallelic Mutations

scholarly journals Tetratricopeptide repeat domain 9A modulates anxiety-like behavior in female mice

2016 ◽  
Vol 6 (1) ◽  
Author(s):  
Lee Wei Lim ◽  
Smeeta Shrestha ◽  
Yu Zuan Or ◽  
Shawn Zheng Kai Tan ◽  
Hwa Hwa Chung ◽  
...  
Keyword(s):  
Tetratricopeptide Repeat ◽  
Female Mice ◽  
Repeat Domain ◽  
Tetratricopeptide Repeat Domain
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