461:. Zhang and colleagues demonstrated that USPs may be involved in the promotion of intertidal biofilms. They observed that during stressful conditions involving metal ions and oxidative stresses that the biofilm phenotype would form. Upon analysis of these biofilms, it could be seen that there was a greatly upregulated level of UspA which Zhang suggests, may be involved with induction of biofilm formation. It is thought UspA may be involved in signalling processes which will upregulate genes involved with biofilm production. With findings such as these, it's beginning to be accepted that USPs are acting using an extremely wide range of mechanisms to ensure cell survival.
367:
protein family. This is due to the similarity in structure between many distantly related organisms. Aravind et al. confirmed these ideas with extensive evolutionary analysis. Aravind suggested that these proteins were part of a much larger protein structural family which was present and diversified in our last universal common ancestor for all extant life. The original function has been suggested to be a nucleotide binding domain which was implicated in signal transduction
261:
26:
473:. This includes sigma factor Ο70 which through binding to a single promoter region, upregulates the transcription of UspA in bacteria. The genes are regulated in a monocistronic fashion. Additionally, UspA, UspC, UspD and UspE are over induced during stationary phase through regulation of RecA. RecA is known for its involvement in the repair of DNA via
644:, as well as an additional 50 genes involved in long-term persistence in the mammalian host. It was suggested this USP gene was involved in inducing the latent response within the mammalian host. This stage of the infection is currently chronic with no effective treatments. This makes these kinds of findings extremely valuable.
481:. Consequently, the four Usp domain genes are thought to be mediating the management or protection of DNA. Whatever the mechanism exhibited by the proteins, one thing which can be concluded is that USP domains are crucial for survival of many bacterial species. Gomes et al. found that UspA deletions in
652:
aiding the diagnostic process for TB. Therefore, these USP genes could be crucial for the long-term survival of the bacteria, meaning that there may be potential therapeutic avenues of research to explore in treating latent TB. This comes at a time whereby TB kills many thousands of people a day and
586:. These granuloma structures are made up of various cellular materials and immune cells. These include macrophages, neutrophils, cellulose and fats. It has long been proposed that USPs play a significant role in the persistence of TB within the human host. This is due to observations of elevated
423:
UspA is the most commonly studied USP due to its widespread presence within bacterial genomes. UspA is especially implicated in the resistance of a huge number of stressors most notably tetracycline exposure and high temperatures, with the exception of not forming a response to cold shock. It is
366:
The ubiquitous nature of these proteins suggests the domain evolved in an ancestral species as well as highlighting the clear biological significance these proteins have in order to still be present in the three domains of life. It has been suggested that the USP A domain was part of an ancient
693:
assisting in survival and hence, pathogenicity. When UspA is inactivated in
Salmonella, the mutants die prematurely, demonstrating how crucial these proteins are to survival and persistence. Again, understanding these processes may aid researchers in developing effective drugs to treat these
428:
following starvation of nutrients. UspA during normal growth conditions does not seem to influence gene expression. However, during stressful conditions such as carbon starvation, UspA has been shown to have a global influence on gene expression. A proposed mechanism for such a change in
445:
550:. These actions are suggested to occur due to their implications in increasing energy conservation. Water limiting conditions are a common environmental pressure which plants will need to cope with on a regular basis, depending on their habitat. These resistant
394:
binding activity. However, as it is such a diverse group, often with little known about the exact structure, itβs not possible to comment on each USP. In addition to this, UspA may reside in different areas of the cell. For example, in this case it was in the
647:
Rv2623 has an ATP binding domain which if knocked out results in a hyper-virulent form of the bacteria. Understanding these processes aids researchers in their quest to provide effective treatment for those suffering from TB. Rv2623 is also a key
419:
there are six families of USP domains which are present in more than 1000 different proteins. The six families are Usp A, -C, -D, -E, -F and βG which are triggered by differing environmental insults and often act via varying mechanisms.
582:(TB), persists within an estimated two billion people. TB is known for its ability to transition into a latent state whereby there is slow growth but high persistence within the mammalian host in structures known as
229:. Proteins containing the domain are induced by many environmental stressors such as nutrient starvation, drought, extreme temperatures, high salinity, and the presence of uncouplers, antibiotics and metals.
456:
The induction of USP proteins have also been implicated in transitions not only in metabolism or growth but in changes in the colonies' entire phenotype. Bacterial colonies can produce formations known as
358:
across the cell membrane. This demonstrates how versatile USPs can be. Their function, while primarily encompasses increasing survival during stressful conditions, is not always limited to this.
981:
Aravind L, et al. (2002). "Monophyly of class I aminoacyl tRNA synthetase, USPA, ETFP, photolyase, and PP-ATPase nucleotide-binding domains: implications for protein evolution in the RNA".
940:
Schweikhard ES, et al. (2010). "Structure and function of the universal stress protein TeaD and its role in regulating the ectoine transporter TeaABC of
Halomonas elongata DSM 2581(T)".
640:
which are particularly prevalent within the granuloma structures that are characteristic of TB latent infections. These conditions have been found to upregulate a particular USP gene called
1360:
Diez A (2002). "The universal stress protein A of
Escherichia coli is required for resistance to DNA damaging agents and is regulated by a RecA/FtsK-dependent regulatory pathway".
689:
by ppGpp and RecA. These responses have been suggested to be involved in the protection of DNA. As a result, UspA aids
Salmonella to resist stressors produced by the mammalian
673:, food poisoning of this kind is a potentially life-threatening condition. The USPs have influence in growth arrest, stress responses and virulence. UspA is induced by
141:
305:
Recent research also suggests proteins containing this domain have functions beyond the realms of dealing with environmental stresses. Nachin et al. demonstrated in
437:
becomes far more vulnerable UV induced DNA damage. Itβs important to note the USP responses are independent of many other stress responses seen in bacteria such as
1639:"Mycobacterium tuberculosis universal stress protein Rv2623 regulates bacillary growth by ATP-Binding: requirement for establishing chronic persistent infection"
1216:
Gustavsson N (2002). "The universal stress protein paralogues of
Escherichia coli are co-ordinately regulated and co-operate in the defence against DNA damage".
448:
This schematic shows a generalised bacterial response to an environmental stress. In this case, it depicts increased levels of Nitric Oxide which stimulates
252:
to better cope with stresses by largely unknown mechanisms. However, the USPs will alter the expression of a variety of genes that help to cope with stress.
1407:"Universal Stress Proteins Are Important for Oxidative and Acid Stress Resistance and Growth of Listeria monocytogenes EGD-e In Vitro and In Vivo"
452:
gene transcription. This results in an anti-stress response from the cell which may or may not include the responses listed within the diagram.
89:
711:
Tan K, et al. (2008). "The crystal structure of an universal stress protein UspA family protein from
Lactobacillus plantarum WCFS1".
1695:
25:
654:
1362:
1218:
890:"Differential Roles of the Universal Stress Proteins of Escherichia coli in Oxidative Stress Resistance, Adhesion, and Motility"
609:
results in USP binding activity with intracellular cAMP which has indirect implications on transcription within the bacteria.
161:
339:
were shown to have enhanced swimming abilities. Therefore, mobility is affected both positively and negatively USPs within
331:, saw results suggesting an inability to swim and completely lack of motility, respectively. Conversely, mutants for genes
375:
As the USP domain is widespread across many organisms, there is great diversity in the structures of these proteins. For
554:
will have an increased survival as they allow the plant to conserve energy in times of restricted water which is key to
383:
with characteristic alpha and beta fold structures. There are differences among different bacteria in areas such as
686:
575:
539:
occurs, biochemical changes induced by the actions of USPs ensue. In response to drought, there is a reduction in
531:
contain many hundreds of USP domains and genes. These genes are notably induced by environmental stresses such as
1873:
1868:
1798:
Liu WT (2007). "Role of the universal stress protein UspA of
Salmonella in growth arrest, stress and virulence".
1027:
Becker JD (2001). "The nodulin vfENOD18 is an ATP-binding protein in infected cells of Vicia faba L. nodules".
804:
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390:. In this case, UspA does not have ATP binding activity. Generally, USPs form dimers and have domains for
384:
1079:
605:, these USPs are regulated by FtsK and FadR. One recent finding shows that the induction of USPs within
145:
1418:
1279:
858:
Sousa MC (2001). "Structure of
Haemophylus influenzae Universal Stress Protein At 1.85A Resolution".
813:
670:
272:
102:
1744:"Individual Mycobacterium tuberculosis universal stress protein homologues are dispensable in vitro"
343:. This demonstrates USPs influence throughout the cell could be widespread for a number of reasons.
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dependent regulatory pathways. USP domain genes are also under the negative control of FadR.
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1266:"Adaptation of intertidal biofilm communities is driven by metal ion and oxidative stresses"
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Kvint K (2013). "The bacterial universal stress protein: function and regulation".
625:
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124:
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1838:
1656:
1494:"Identification of drought-responsive universal stress proteins in viridiplantae"
1431:
415:(Strain K-12). Consequently, much is known about the USP domains in bacteria. In
82:
682:
637:
497:
295:
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1543:
Ramakrishnan L (2012). "Revisiting the role of the granuloma in tuberculosis".
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conditions found within the granuloma. Specifically, Rv2623, a type of USP in
583:
551:
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478:
391:
1709:
800:"Structural and functional insight into the universal stress protein family"
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350:, there is a USP called TeaD has been described as a key regulator in the
98:
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636:. All of these conditions are suggested to be produced by the actions of
601:, all of which have an ATP binding domain. It has been found that within
486:
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276:
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The primary function of this superfamily is to protect the organism from
237:
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77:
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related stress. In these conditions UspA is over produced through the
433:
is that UspA has been suggested to bind to DNA. When UspA is mutated,
1075:"Structure of the universal stress protein of Haemophilus influenzae"
543:
528:
496:
USP domain genes are regulated by a number of proteins involved with
379:, its UspA resides in the cytoplasm. The protein forms an asymmetric
226:
156:
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severely impaired survival as well as listeriaβs stress response by
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In bacteria, the USP genes can be regulated by sigma factors within
509:
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438:
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Much of the research into USP is done on bacteria, specifically
118:
64:
52:
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1691:"A Universal Stress Protein (USP) in Mycobacteria binds cAMP"
653:
is becoming increasing problematic to treat with the rise of
264:
The protein structure of a
Universal Stress Protein found in
633:
236:
genes are upregulated resulting in large quantities of Usp
1593:"Universal stress proteins and Mycobacterium tuberculosis"
1172:"Universal stress proteins and Mycobacterium tuberculosis"
1211:
1209:
424:
thought UspA is especially important to the recovery of
287:
and more generally the cell from further damage. During
508:. Notable positive regulation occurs via the action of
1259:
1257:
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155:
135:
117:
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76:
63:
51:
43:
38:
18:
283:containing the USP domain in order to protect the
1114:
1112:
1839:WikiGenes: UspA - The universal stress regulator
1586:
1584:
665:Similarly, USPs are crucial for the survival of
594:in the latent granuloma stage of the infection.
748:"Universal Stress Proteins in Escherichia coli"
741:
739:
737:
735:
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731:
1487:
1485:
298:and promote its metabolism to adapt to sparse
8:
294:the USP genes upregulated will often arrest
1632:
1630:
669:, the causative agent in Salmonellosis. In
311:that USPs are involved in actions such as
109:
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616:USPs are suggested to be induced by the
443:
259:
703:
578:, the infectious agent responsible for
15:
597:There are eight types of USPs within
546:production as well as a reduction in
7:
1121:"The Pfam protein families database"
319:. The researchers, through means of
232:In the presence of these stressors,
1696:The Journal of Biological Chemistry
14:
399:but for others, it may be in the
1465:"The Universal Stress Protein A"
1376:10.1046/j.1365-2958.2000.01979.x
1232:10.1046/j.1365-2958.2002.02720.x
908:10.1128/JB.187.18.6265-6272.2005
798:Tkaczuk KL, et al. (2013).
766:10.1128/jb.187.18.6253-6254.2005
746:Siegele DA, et al. (2005).
624:, is induced by the presence of
24:
888:Nachin L, et al. (2005).
1:
1844:PortEco: Gene Database - UspA
1814:10.1016/j.micpath.2006.09.002
1612:10.1016/S0923-2508(03)00081-0
1339:10.1016/S1369-5274(03)00025-0
1191:10.1016/S0923-2508(03)00081-0
1094:10.1016/s0969-2126(01)00680-3
244:. The over production of USP
113:Available protein structures:
1657:10.1371/journal.ppat.1000460
1432:10.1371/journal.pone.0024965
30:UspA protein structure from
1895:
1762:10.1016/j.tube.2010.03.013
1742:Hingley-Wilson SM (2010).
687:transcriptional regulation
576:Mycobacterium tuberculosis
19:Universal Stress Protein A
805:Evolutionary Applications
108:
23:
1598:Research in Microbiology
1177:Research in Microbiology
475:homologous recombination
195:universal stress protein
1710:10.1074/jbc.M115.644856
1499:bioinform Biol Insights
1043:10.1023/A:1013664311052
895:Journal of Bacteriology
753:Journal of Bacteriology
655:multi-drug-resistant TB
630:reactive oxygen species
32:Lactobacillus plantarum
1854:EMBL-EBI Pfam for UspA
1801:Microbial Pathogenesis
1363:Molecular Microbiology
1219:Molecular Microbiology
1126:Nucleic Acids Research
453:
377:Haemophilus influenzae
268:
266:Haemophylus influenzae
240:being produced by the
209:which can be found in
1471:. Uniprot. 2015-03-25
566:Clinical significance
447:
263:
1492:Isokpehi RD (2011).
671:developing countries
275:such as exposure to
273:environmental stress
1689:Banerjee A (2015).
1423:2011PLoSO...624965S
1326:Curr Opin Microbiol
1284:2013NatSR...3E3180Z
1080:Bichemical Sciences
874:10.2210/pdb1jmv/pdb
818:2013EvApp...6..434T
721:10.2210/pdb3fg9/pdb
632:and a downshift in
558:production through
323:USP genes known as
279:, which may induce
1849:PDB UspA Structure
1591:O'Toole R (2003).
1271:Scientific Reports
1170:O'Toole R (2003).
1139:10.1093/nar/gkh121
1133:(90001): 138β141.
1119:Bateman A (2004).
997:10.1002/prot.10064
454:
269:
1637:Drumm JE (2009).
1512:10.4137/BBI.S6061
1405:Gomes CS (2011).
1292:10.1038/srep03180
1087:(12): 1135β1141.
1073:Sousa MC (2001).
956:10.1021/bi9017522
950:(10): 2194β2204.
902:(18): 6265β6272.
826:10.1111/eva.12057
760:(18): 6253β6254.
713:Protein Data Bank
548:energy metabolism
535:. When a lack of
348:Halmonas elongate
346:Additionally, in
191:
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162:structure summary
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1874:Stress (biology)
1869:Protein families
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1264:Zhang W (2013).
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1749:Tuberculosis
1747:
1737:
1703:(20): 1β28.
1700:
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1644:PLoS Pathog.
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626:nitric oxide
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580:tuberculosis
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31:
1808:(1): 2β10.
991:(1): 1β14.
683:temperature
638:macrophages
296:cell growth
248:allows the
203:superfamily
39:Identifiers
1863:Categories
1475:2015-03-25
698:References
667:Salmonella
661:Salmonella
584:granulomas
552:phenotypes
502:DNA repair
477:following
465:Regulation
392:nucleotide
292:starvation
125:structures
1506:: 41β58.
861:Structure
679:oxidative
675:metabolic
650:biomarker
537:hydration
397:cytoplasm
371:Structure
362:Evolution
352:transport
300:nutrients
289:bacterial
250:organisms
83:IPR006016
1879:Genetics
1822:17081727
1780:20541977
1729:25802331
1676:19478878
1621:12892844
1567:22517424
1530:21423406
1451:21980369
1411:PLOS ONE
1392:22239740
1384:10931298
1347:12732303
1310:24212283
1278:: 3180.
1248:25979289
1240:11849540
1200:12892844
1157:14681378
1103:11738040
1059:24974722
1051:11785936
1013:32908067
1005:12012333
964:20113006
926:16159758
844:23745136
784:16159755
612:Some of
487:in vitro
483:Listeria
459:biofilms
407:Bacteria
317:motility
313:adhesion
277:UV light
256:Function
238:proteins
223:protozoa
211:bacteria
142:RCSB PDB
78:InterPro
1771:2914252
1720:4432290
1667:2682197
1575:1139969
1521:3045048
1442:3184099
1419:Bibcode
1301:3822395
1280:Bibcode
984:Protein
917:1236625
835:3673472
814:Bibcode
775:1236659
618:hypoxic
556:glucose
533:drought
491:in vivo
435:E. coli
426:E. coli
417:E. coli
413:E. coli
356:Ectoine
341:E. coli
215:archaea
58:PF00582
47:lp_3663
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642:rv2623
544:carbon
529:Plants
524:Plants
498:growth
479:damage
227:plants
157:PDBsum
131:
121:
103:SUPFAM
44:Symbol
1571:S2CID
1388:S2CID
1244:S2CID
1055:S2CID
1009:S2CID
510:ppGpp
381:dimer
281:genes
246:genes
219:fungi
99:SCOPe
90:SCOP2
1818:PMID
1776:PMID
1725:PMID
1672:PMID
1617:PMID
1563:PMID
1526:PMID
1447:PMID
1380:PMID
1343:PMID
1306:PMID
1236:PMID
1196:PMID
1153:PMID
1099:PMID
1047:PMID
1001:PMID
960:PMID
922:PMID
840:PMID
780:PMID
681:and
518:FtsZ
516:and
514:RecA
504:and
489:and
439:rpoS
337:UspG
335:and
333:UspF
329:UspC
327:and
325:UspE
315:and
242:cell
225:and
193:The
181:3S3T
178:1JMV
175:3FG9
150:PDBj
146:PDBe
129:ECOD
119:Pfam
95:1mjh
67:clan
65:Pfam
53:Pfam
1810:doi
1766:PMC
1758:doi
1715:PMC
1705:doi
1662:PMC
1652:doi
1607:doi
1603:154
1555:doi
1516:PMC
1508:doi
1437:PMC
1427:doi
1372:doi
1335:doi
1296:PMC
1288:doi
1228:doi
1186:doi
1182:154
1143:PMC
1135:doi
1089:doi
1039:doi
993:doi
952:doi
912:PMC
904:doi
900:187
870:doi
830:PMC
822:doi
770:PMC
762:doi
758:187
717:doi
588:Usp
450:Usp
385:ATP
354:of
285:DNA
234:Usp
205:of
199:USP
169:PDB
137:PDB
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