scholarly journals 3D Structure and Function of Glycosyltransferases Involved in N-glycan Maturation

2020 ◽  
Vol 21 (2) ◽  
pp. 437 ◽  
Author(s):  
Masamichi Nagae ◽  
Yoshiki Yamaguchi ◽  
Naoyuki Taniguchi ◽  
Yasuhiko Kizuka
Keyword(s):  
Reaction Mechanisms ◽  
Recent Progress ◽  
Protein Transport ◽  
3D Structure ◽  
Biological Significance ◽  
Structure And Function ◽  
Glycan Structure ◽  
Post Translational Modification ◽  
Biochemical Studies ◽  
And Function

Glycosylation is the most ubiquitous post-translational modification in eukaryotes. N-glycan is attached to nascent glycoproteins and is processed and matured by various glycosidases and glycosyltransferases during protein transport. Genetic and biochemical studies have demonstrated that alternations of the N-glycan structure play crucial roles in various physiological and pathological events including progression of cancer, diabetes, and Alzheimer’s disease. In particular, the formation of N-glycan branches regulates the functions of target glycoprotein, which are catalyzed by specific N-acetylglucosaminyltransferases (GnTs) such as GnT-III, GnT-IVs, GnT-V, and GnT-IX, and a fucosyltransferase, FUT8s. Although the 3D structures of all enzymes have not been solved to date, recent progress in structural analysis of these glycosyltransferases has provided insights into substrate recognition and catalytic reaction mechanisms. In this review, we discuss the biological significance and structure-function relationships of these enzymes.

scholarly journals Intrinsic disorder in protein domains contributes to both organism complexity and clade-specific functions

2021 ◽  
Vol 11 (1) ◽  
Author(s):  
Chao Gao ◽  
Chong Ma ◽  
Huqiang Wang ◽  
Haolin Zhong ◽  
Jiayin Zang ◽  
...  
Keyword(s):  
Biological Significance ◽  
Protein Domains ◽  
Functional Requirements ◽  
Post Translational Modification ◽  
Intrinsically Disordered ◽  
Genome Wide ◽  
Complex Functions ◽  
Disorder Degree ◽  
Functional Features ◽  
And Function

AbstractInterestingly, some protein domains are intrinsically disordered (abbreviated as IDD), and the disorder degree of same domains may differ in different contexts. However, the evolutionary causes and biological significance of these phenomena are unclear. Here, we address these issues by genome-wide analyses of the evolutionary and functional features of IDDs in 1,870 species across the three superkingdoms. As the result, there is a significant positive correlation between the proportion of IDDs and organism complexity with some interesting exceptions. These phenomena may be due to the high disorder of clade-specific domains and the different disorder degrees of the domains shared in different clades. The functions of IDDs are clade-specific and the higher proportion of post-translational modification sites may contribute to their complex functions. Compared with metazoans, fungi have more IDDs with a consecutive disorder region but a low disorder ratio, which reflects their different functional requirements. As for disorder variation, it’s greater for domains among different proteins than those within the same proteins. Some clade-specific ‘no-variation’ or ‘high-variation’ domains are involved in clade-specific functions. In sum, intrinsic domain disorder is related to both the organism complexity and clade-specific functions. These results deepen the understanding of the evolution and function of IDDs.

The axonemal microtubules of the Chlamydomonas flagellum differ in tubulin isoform content

1998 ◽  
Vol 111 (3) ◽  
pp. 313-320 ◽  
Author(s):  
K.A. Johnson
Keyword(s):  
Structure And Function ◽  
Post Translational Modification ◽  
Immunofluorescence Analysis ◽  
Central Pair ◽  
Alpha Tubulin ◽  
Microtubule Polymerization ◽  
Tubulin Isoforms ◽  
Flagellar Assembly ◽  
Tyrosinated Tubulin ◽  
And Function

Little is known of the molecular basis for the diversity of microtubule structure and function found within the eukaryotic flagellum. Antibodies that discriminate between tyrosinated alpha tubulin and post-translationally detyrosinated alpha tubulin were used to localize these complementary tubulin isoforms in flagella of the single-celled green alga Chlamydomonas reinhardtii. Immunofluorescence analysis of intact axonemes detected both isoforms along most of the lengths of flagella; however, each had a short distal zone rich in tyrosinated tubulin. Localizations on splayed axonemes revealed that the microtubules of the central-pair apparatus were rich in tyrosinated tubulin, while outer doublets contained a mixture of both isoforms. Immunoelectron analysis of individual outer doublets revealed that while tyrosinated tubulin was present in both A and B tubules, detyrosinated tubulin was largely confined to the wall of the B hemi-tubules. The absence of detyrosinated tubulin from the A tubules of the outer doublets and the microtubules of the central pair, both of which extend past the B hemi-tubules of the outer doublets in the flagellar tip, explained the appearance of a tyrosinated tubulin-rich distal zone on intact axonemes. Localizations performed on cells regenerating flagella revealed that flagellar assembly used tyrosinated tubulin; detyrosination of the B tubule occurred during later stages of regeneration, well after microtubule polymerization. The developmental timing of detyrosination, which occurs over a period during which the regrowing flagella begin to beat more effectively, suggests that post-translational modification of the B tubule surface may enhance dynein/B tubule interactions that power flagellar beating.

Recent Progress in Hormone Research, Vol. XIV. The Proceedings of the Laurentian Hormone Conference

PEDIATRICS ◽  
1959 ◽  
Vol 23 (5) ◽  
pp. 961-961
Author(s):  
LYTT I. GARDNER
Keyword(s):  
Special Interest ◽  
Growth And Development ◽  
Recent Progress ◽  
Structure And Function ◽  
Hormone Research ◽  
And Function

This is the 14th volume of this valuable series of the Laurentian Hormone Conference. The editor continues the same excellent format as in the previous volumes. There are 14 monographs on various aspects of endocrinology each followed by a bibliography and verbatim record of the discussion. The volume is divided into five sections: I. Hormone Structure and Function; II. Hormones in Growth and Development; III. Aspects of Reproduction; IV. Hormones and Metabolism; and V. Neurohumors. Of special interest to pediatricians is the section on cytologic tests of chromosomal sex by Grumbach and Barr.

scholarly journals Deciphering the 3D Structure and Function of Phosphofructokinase from Fission Yeast

2014 ◽  
Vol 20 (S3) ◽  
pp. 1246-1247
Author(s):  
Shaun Benjamin ◽  
Michael Radermacher ◽  
Teresa Ruiz
Keyword(s):  
Fission Yeast ◽  
3D Structure ◽  
Structure And Function ◽  
And Function

Native Mass Spectrometry: Recent Progress and Remaining Challenges

2022 ◽  
Vol 51 (1) ◽  
Author(s):  
Kelly R. Karch ◽  
Dalton T. Snyder ◽  
Sophie R. Harvey ◽  
Vicki H. Wysocki
Keyword(s):  
Mass Spectrometry ◽  
Gas Phase ◽  
Structural Biology ◽  
Recent Progress ◽  
Native Mass Spectrometry ◽  
Structure And Function ◽  
Annual Review ◽  
Publication Date ◽  
Analysis Software ◽  
And Function

Native mass spectrometry (nMS) has emerged as an important tool in studying the structure and function of macromolecules and their complexes in the gas phase. In this review, we cover recent advances in nMS and related techniques including sample preparation, instrumentation, activation methods, and data analysis software. These advances have enabled nMS-based techniques to address a variety of challenging questions in structural biology. The second half of this review highlights recent applications of these technologies and surveys the classes of complexes that can be studied with nMS. Complementarity of nMS to existing structural biology techniques and current challenges in nMS are also addressed. Expected final online publication date for the Annual Review of Biophysics, Volume 51 is May 2022. Please see http://www.annualreviews.org/page/journal/pubdates for revised estimates.

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