Next Issue
Previous Issue

Table of Contents

Biomolecules, Volume 2, Issue 2 (June 2012), Pages 187-311

  • Issues are regarded as officially published after their release is announced to the table of contents alert mailing list.
  • You may sign up for e-mail alerts to receive table of contents of newly released issues.
  • PDF is the official format for papers published in both, html and pdf forms. To view the papers in pdf format, click on the "PDF Full-text" link, and use the free Adobe Readerexternal link to open them.
View options order results:
result details:
Displaying articles 1-8
Export citation of selected articles as:

Research

Jump to: Review, Other

Open AccessArticle Genetic Fingerprinting of Wheat and Its Progenitors by Mitochondrial Gene orf256
Biomolecules 2012, 2(2), 228-239; doi:10.3390/biom2020228
Received: 15 March 2012 / Revised: 29 March 2012 / Accepted: 4 April 2012 / Published: 13 April 2012
Cited by 1 | PDF Full-text (310 KB) | HTML Full-text | XML Full-text
Abstract
orf256 is a wheat mitochondrial gene associated with cytoplasmic male sterility (CMS) that has different organization in various species. This study exploited the orf256 gene as a mitochondrial DNA marker to study the genetic fingerprint of Triticum and Aegilops species. PCR followed by
[...] Read more.
orf256 is a wheat mitochondrial gene associated with cytoplasmic male sterility (CMS) that has different organization in various species. This study exploited the orf256 gene as a mitochondrial DNA marker to study the genetic fingerprint of Triticum and Aegilops species. PCR followed by sequencing of common parts of the orf256 gene were employed to determine the fingerprint and molecular evolution of Triticum and Aegilops species. Although many primer pairs were used, two pairs of orf256 specific primers (5:-94/C: 482, 5:253/C: 482), amplified DNA fragments of 576 bp and 230 bp respectively in all species were tested. A common 500 bp of nine species of Triticum and Aegilops were aligned and showed consistent results with that obtained from other similar chloroplast or nuclear genes. Base alignment showed that there were various numbers of base substitutions in all species compared to S. cereal (Sc) (the outgroup species). Phylogenetic relationship revealed similar locations and proximity on phylogenetic trees established using plastid and nuclear genes. The results of this study open a good route to use unknown function genes of mitochondria in studying the molecular relationships and evolution of wheat and complex plant genomes. Full article
Figures

Open AccessArticle DeSUMOylation Controls Insulin Exocytosis in Response to Metabolic Signals
Biomolecules 2012, 2(2), 269-281; doi:10.3390/biom2020269
Received: 3 May 2012 / Revised: 14 May 2012 / Accepted: 16 May 2012 / Published: 24 May 2012
Cited by 4 | PDF Full-text (475 KB) | HTML Full-text | XML Full-text
Abstract
The secretion of insulin by pancreatic islet β-cells plays a pivotal role in glucose homeostasis and diabetes. Recent work suggests an important role for SUMOylation in the control of insulin secretion from β-cells. In this paper we discuss mechanisms whereby (de)SUMOylation may control
[...] Read more.
The secretion of insulin by pancreatic islet β-cells plays a pivotal role in glucose homeostasis and diabetes. Recent work suggests an important role for SUMOylation in the control of insulin secretion from β-cells. In this paper we discuss mechanisms whereby (de)SUMOylation may control insulin release by modulating β-cell function at one or more key points; and particularly through the acute and reversible regulation of the exocytotic machinery. Furthermore, we postulate that the SUMO-specific protease SENP1 is an important mediator of insulin exocytosis in response to NADPH, a metabolic secretory signal and major determinant of β-cell redox state. Dialysis of mouse β-cells with NADPH efficiently amplifies β-cell exocytosis even when extracellular glucose is low; an effect that is lost upon knockdown of SENP1. Conversely, over-expression of SENP1 itself augments β-cell exocytosis in a redox-dependent manner. Taken together, we suggest that (de)SUMOylation represents an important mechanism that acutely regulates insulin secretion and that SENP1 can act as an amplifier of insulin exocytosis. Full article
(This article belongs to the Special Issue Protein SUMOylation)
Figures

Review

Jump to: Research, Other

Open AccessReview Cell Penetrating Peptides in the Delivery of Biopharmaceuticals
Biomolecules 2012, 2(2), 187-202; doi:10.3390/biom2020187
Received: 1 March 2012 / Revised: 16 March 2012 / Accepted: 23 March 2012 / Published: 30 March 2012
Cited by 26 | PDF Full-text (248 KB) | HTML Full-text | XML Full-text
Abstract
The cell membrane is a highly selective barrier. This limits the cellular uptake of molecules including DNA, oligonucleotides, peptides and proteins used as therapeutic agents. Different approaches have been employed to increase the membrane permeability and intracellular delivery of these therapeutic molecules. One
[...] Read more.
The cell membrane is a highly selective barrier. This limits the cellular uptake of molecules including DNA, oligonucleotides, peptides and proteins used as therapeutic agents. Different approaches have been employed to increase the membrane permeability and intracellular delivery of these therapeutic molecules. One such approach is the use of Cell Penetrating Peptides (CPPs). CPPs represent a new and innovative concept, which bypasses the problem of bioavailability of drugs. The success of CPPs lies in their ability to unlock intracellular and even intranuclear targets for the delivery of agents ranging from peptides to antibodies and drug-loaded nanoparticles. This review highlights the development of cell penetrating peptides for cell-specific delivery strategies involving biomolecules that can be triggered spatially and temporally within a cell transport pathway by change in physiological conditions. The review also discusses conjugations of therapeutic agents to CPPs for enhanced intracellular delivery and bioavailability that are at the clinical stage of development. Full article
Open AccessReview Sumoylation at the Host-Pathogen Interface
Biomolecules 2012, 2(2), 203-227; doi:10.3390/biom2020203
Received: 21 February 2012 / Revised: 21 March 2012 / Accepted: 27 March 2012 / Published: 5 April 2012
Cited by 11 | PDF Full-text (680 KB) | HTML Full-text | XML Full-text
Abstract
Many viral proteins have been shown to be sumoylated with corresponding regulatory effects on their protein function, indicating that this host cell modification process is widely exploited by viral pathogens to control viral activity. In addition to using sumoylation to regulate their own
[...] Read more.
Many viral proteins have been shown to be sumoylated with corresponding regulatory effects on their protein function, indicating that this host cell modification process is widely exploited by viral pathogens to control viral activity. In addition to using sumoylation to regulate their own proteins, several viral pathogens have been shown to modulate overall host sumoylation levels. Given the large number of cellular targets for SUMO addition and the breadth of critical cellular processes that are regulated via sumoylation, viral modulation of overall sumoylation presumably alters the cellular environment to ensure that it is favorable for viral reproduction and/or persistence. Like some viruses, certain bacterial plant pathogens also target the sumoylation system, usually decreasing sumoylation to disrupt host anti-pathogen responses. The recent demonstration that Listeria monocytogenes also disrupts host sumoylation, and that this is required for efficient infection, extends the plant pathogen observations to a human pathogen and suggests that pathogen modulation of host sumoylation may be more widespread than previously appreciated. This review will focus on recent aspects of how pathogens modulate the host sumoylation system and how this benefits the pathogen. Full article
(This article belongs to the Special Issue Protein SUMOylation)
Figures

Open AccessReview The Role of the Small Ubiquitin-Related Modifier (SUMO) Pathway in Prostate Cancer
Biomolecules 2012, 2(2), 240-255; doi:10.3390/biom2020240
Received: 15 March 2012 / Revised: 28 March 2012 / Accepted: 9 April 2012 / Published: 23 April 2012
PDF Full-text (291 KB) | HTML Full-text | XML Full-text
Abstract
SUMO (small ubiquitin-related modifier) conjugation is a reversible three-step process of protein post-translational modifications mediating protein-protein interactions, subcellular compartmentalization and regulation of transcriptional events. Among divergent transcription factors regulated by SUMOylation and deSUMOylation, the androgen receptor (AR) is of exceptional significance, given its
[...] Read more.
SUMO (small ubiquitin-related modifier) conjugation is a reversible three-step process of protein post-translational modifications mediating protein-protein interactions, subcellular compartmentalization and regulation of transcriptional events. Among divergent transcription factors regulated by SUMOylation and deSUMOylation, the androgen receptor (AR) is of exceptional significance, given its established role in prostate carcinogenesis. The enzymes of the SUMO pathway can have diverse effects on AR transcriptional activity, either via direct modification of the AR or through modification of AR co-regulators. Accumulating in vitro and in vivo evidence implicates the SUMO pathway in AR-dependent signaling. Prostate cancer cell proliferation and hypoxia-induced angiogenesis are also regulated by the SUMO pathway, through an AR-independent mechanism. Thus, an important role has been revealed for members of the SUMO pathway in prostate cancer (PCa) development and progression, offering new therapeutic targets. Full article
(This article belongs to the Special Issue Protein SUMOylation)
Figures

Open AccessReview Regulation of Neuronal Protein Trafficking and Translocation by SUMOylation
Biomolecules 2012, 2(2), 256-268; doi:10.3390/biom2020256
Received: 14 April 2012 / Revised: 24 April 2012 / Accepted: 24 April 2012 / Published: 14 May 2012
Cited by 1 | PDF Full-text (646 KB) | HTML Full-text | XML Full-text
Abstract
Post-translational modifications of proteins are essential for cell function. Covalent modification by SUMO (small ubiquitin-like modifier) plays a role in multiple cell processes, including transcriptional regulation, DNA damage repair, protein localization and trafficking. Factors affecting protein localization and trafficking are particularly crucial in
[...] Read more.
Post-translational modifications of proteins are essential for cell function. Covalent modification by SUMO (small ubiquitin-like modifier) plays a role in multiple cell processes, including transcriptional regulation, DNA damage repair, protein localization and trafficking. Factors affecting protein localization and trafficking are particularly crucial in neurons because of their polarization, morphological complexity and functional specialization. SUMOylation has emerged as a major mediator of intranuclear and nucleo-cytoplasmic translocations of proteins involved in critical pathways such as circadian rhythm, apoptosis and protein degradation. In addition, SUMO-regulated re-localization of extranuclear proteins is required to sustain neuronal excitability and synaptic transmission. Thus, SUMOylation is a key arbiter of neuronal viability and function. Here, we provide an overview of recent advances in our understanding of regulation of neuronal protein localization and translocation by SUMO and highlight exciting areas of ongoing research. Full article
(This article belongs to the Special Issue Protein SUMOylation)
Figures

Open AccessReview Leucine-Rich Repeat (LRR) Domains Containing Intervening Motifs in Plants
Biomolecules 2012, 2(2), 288-311; doi:10.3390/biom2020288
Received: 7 May 2012 / Revised: 13 June 2012 / Accepted: 13 June 2012 / Published: 22 June 2012
Cited by 18 | PDF Full-text (1269 KB) | HTML Full-text | XML Full-text | Supplementary Files
Abstract
LRRs (leucine rich repeats) are present in over 14,000 proteins. Non-LRR, island regions (IRs) interrupting LRRs are widely distributed. The present article reviews 19 families of LRR proteins having non-LRR IRs (LRR@IR proteins) from various plant species. The LRR@IR proteins are LRR-containing receptor-like
[...] Read more.
LRRs (leucine rich repeats) are present in over 14,000 proteins. Non-LRR, island regions (IRs) interrupting LRRs are widely distributed. The present article reviews 19 families of LRR proteins having non-LRR IRs (LRR@IR proteins) from various plant species. The LRR@IR proteins are LRR-containing receptor-like kinases (LRR-RLKs), LRR-containing receptor-like proteins (LRR-RLPs), TONSOKU/BRUSHY1, and MJK13.7; the LRR-RLKs are homologs of TMK1/Rhg4, BRI1, PSKR, PSYR1, Arabidopsis At1g74360, and RPK2, while the LRR-RLPs are those of Cf-9/Cf-4, Cf-2/Cf-5, Ve, HcrVf, RPP27, EIX1, clavata 2, fascinated ear2, RLP2, rice Os10g0479700, and putative soybean disease resistance protein. The LRRs are intersected by single, non-LRR IRs; only the RPK2 homologs have two IRs. In most of the LRR-RLKs and LRR-RLPs, the number of repeat units in the preceding LRR block (N1) is greater than the number of the following block (N2); N1 » N2 in which N1 is variable in the homologs of individual families, while N2 is highly conserved. The five families of the LRR-RLKs except for the RPK2 family show N1 = 8 − 18 and N2 = 3 − 5. The nine families of the LRR-RLPs show N1 = 12 − 33 and N2 = 4; while N1 = 6 and N2 = 4 for the rice Os10g0479700 family and the N1 = 4 − 28 and N2 = 4 for the soybean protein family. The rule of N1 » N2 might play a common, significant role in ligand interaction, dimerization, and/or signal transduction of the LRR-RLKs and the LRR-RLPs. The structure and evolution of the LRR domains with non-LRR IRs and their proteins are also discussed. Full article
(This article belongs to the Special Issue Feature Papers)
Figures

Other

Jump to: Research, Review

Open AccessCommentary From Phosphorous to Arsenic: Changing the Classic Paradigm for the Structure of Biomolecules
Biomolecules 2012, 2(2), 282-287; doi:10.3390/biom2020282
Received: 23 April 2012 / Revised: 16 May 2012 / Accepted: 22 May 2012 / Published: 30 May 2012
Cited by 2 | PDF Full-text (140 KB) | HTML Full-text | XML Full-text
Abstract
Biomolecules are composed primarily of the elements carbon, nitrogen, hydrogen, oxygen, sulfur, and phosphorus. The structured assembly of these elements forms the basis for proteins, nucleic acids and lipids. However, the recent discovery of a new bacterium, strain GFAJ-1 of the Halomonadaceae,
[...] Read more.
Biomolecules are composed primarily of the elements carbon, nitrogen, hydrogen, oxygen, sulfur, and phosphorus. The structured assembly of these elements forms the basis for proteins, nucleic acids and lipids. However, the recent discovery of a new bacterium, strain GFAJ-1 of the Halomonadaceae, has shaken the classic paradigms for the architecture of life. Mounting evidence supports the claim that these bacteria substitute arsenic for phosphorus in macromolecules. Herein, we provide a brief commentary and fuel the debate related to what may be a most unusual organism. Full article

Journal Contact

MDPI AG
Biomolecules Editorial Office
St. Alban-Anlage 66, 4052 Basel, Switzerland
biomolecules@mdpi.com
Tel. +41 61 683 77 34
Fax: +41 61 302 89 18
Editorial Board
Contact Details Submit to Biomolecules
Back to Top